CAZypedia - User contributions [en-ca]

Carbohydrate Binding Module Family 71

2019-12-13T17:14:04Z

Ben Pluvinage:

{{CuratorApproved}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1 ([{{PDBlink}}4CUB 4CUB]). Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 <cite>Singh2014</cite> solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s [[Carbohydrate-binding_modules#Types|type C]] CBMs <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pi interactions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site <cite>Singh2014</cite>.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site ([{{PDBlink}}4CUB 4CUB]). Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized along with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified: The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization: The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:41:02Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s type C CBM <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized along with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:40:16Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s type C CBM <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae''. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:39:34Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71s type C CBM <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:38:54Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the β-fold opposite the N- and C-termini, making CBM71 a type C CBM <cite>Boraston2004</cite>. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:36:20Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the β-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM <cite>Boraston2004</cite>.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:34:45Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM <cite>Boraston2004</cite>.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID [{{PDBlink}}4CUA 4CUA]), CBM71-1 in complex with LacNAc (PDB ID [{{PDBlink}}4CUB 4CUB]) and CBM71-2 (PDB ID [{{PDBlink}}4CU9 4CU9]) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:30:44Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM <cite>Boraston2004</cite>.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the β-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:29:47Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' <cite>Singh2014</cite>. Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM <cite>Boraston2004</cite>.

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase <cite>Cantarel2009</cite> has been fully characterized in parallel with the characterization of CBM71s <cite>Singh2014</cite>. In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates <cite>Singh2014</cite>.

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from ''S. pneumoniae'' <cite>Singh2014</cite>. CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA <cite>Singh2014</cite>. The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:26:04Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==

[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]

The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' (1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow
binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).

[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]

== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3) has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T22:19:39Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==
[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]
The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' (1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
[[File:CBM71-1CatSite.png|thumb|300px|right|'''Figure 2.''' CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).

== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3) has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

File:CBM71-1CatSite.png

2019-04-10T22:18:34Z

Ben Pluvinage: CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.

CBM71-1 binding site. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.

Carbohydrate Binding Module Family 71

2019-04-10T22:17:25Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==
The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' (1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).
[[File:CBM71-1.png|thumb|300px|right|'''Figure 1.''' Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.]]
== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).

== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3) has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

File:CBM71-1.png

2019-04-10T22:14:54Z

Ben Pluvinage: Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.

Structure of CBM71-1. Cartoon representation of CBM71-1 in complex with LacNAc (green sticks). Color ramped red to blue from N- to C-terminus. A bound calcium atom is shown in magenta.

Carbohydrate Binding Module Family 71

2019-04-10T21:56:28Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==
The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' (1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).

== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3) has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel2009 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T21:48:42Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==
The CBM family 71 was created in September 2014 with the characterization of the large multimodular β-galactosidase BgaA from ''Streptococcus pneumoniae'' (1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-β-1,4-D-glucose) and LacNAc (galactopyranosyl-β-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a β-sandwich fold comprising opposing sheets of 4- and 5-antiparallel β-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both β-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).

== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from ''S. pneumoniae'' BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3) has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).

== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the β-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal β-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel209 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]

Carbohydrate Binding Module Family 71

2019-04-10T21:41:50Z

Ben Pluvinage:

{{UnderConstruction}}
* [[Author]]: ^^^Ben Pluvinage^^^
* [[Responsible Curator]]: ^^^Al Boraston^^^
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM71.html
|}
</div>


== Ligand specificities ==
The CBM family 71 was created in September 2014 with the characterization of the large multimodular b-galactosidase BgaA from Streptococcus pneumoniae(1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-b-1,4-D-glucose) and LacNAc (galactopyranosyl-b-1,4-N-acetyl-D-glucosamine).

== Structural Features ==
The structure of CBM71-1 solved by X-ray crystallography shows a b-sandwich fold comprising opposing sheets of 4- and 5-antiparallel b-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both b-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).
== Functionalities ==
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from S. pneumoniae. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3)has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).
== Family Firsts ==
;First Identified
The CBM71 modules were first identified through the characterization of the b-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
;First Structural Characterization
The first crystal structures of family CBM71s were from the streptococcal b-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

== References ==
<biblio>
#Singh2014 pmid=25210925
#Boraston2004 pmid=15214846
#Cantarel209 pmid=18838391
</biblio>

[[Category:Carbohydrate Binding Module Families|CBM071]]