Carbohydrate Binding Module Family 71 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:14:47Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Ben Pluvinage at 17:14, 13 December 2019

2019-12-13T17:14:04Z

Al Boraston at 16:55, 13 December 2019

2019-12-13T16:55:55Z

Elizabeth Ficko-Blean at 15:04, 11 December 2019

2019-12-11T15:04:00Z

Elizabeth Ficko-Blean at 15:03, 11 December 2019

2019-12-11T15:03:32Z

Elizabeth Ficko-Blean at 14:59, 11 December 2019

2019-12-11T14:59:23Z

Ben Pluvinage at 22:41, 10 April 2019

2019-04-10T22:41:02Z

Ben Pluvinage at 22:40, 10 April 2019

2019-04-10T22:40:16Z

Ben Pluvinage at 22:39, 10 April 2019

2019-04-10T22:39:34Z

Ben Pluvinage at 22:38, 10 April 2019

2019-04-10T22:38:54Z

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]: ^^^Ben Pluvinage^^^
+* [[Author]]: [[User:Ben Pluvinage|Ben Pluvinage]]
-* [[Responsible Curator]]:  ^^^Al Boraston^^^
+* [[Responsible Curator]]:  [[User:Al Boraston|Al Boraston]]
 ----

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 == 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.]]
+[[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).
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 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. Residues involved in binding LacNAc (green) are shown as cyan sticks and waters as red spheres. Black dashed lines represent hydrogen bonds.]]
+[[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 ==

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: ^^^Ben Pluvinage^^^
 * [[Responsible Curator]]:  ^^^Al Boraston^^^

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 == 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>.
+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 ==

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 == 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
+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.
+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. 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>.
+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 ==

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 == 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.
+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.
 [[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.]]
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 == Family Firsts ==
-;First Identified
+;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.
-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 ==