Difference between revisions of "Carbohydrate Binding Module Family 105"

Latest revision as of 20:33, 6 November 2024

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Ligand specificities

The first member of family CBM105 (SoCBM105) was identified in the PL29 multidomain chondroitinase SoChABC29 from Segatella oris [1]. SoCBM105 bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while it was incapable of binding to other glycosaminoglycans or polyuronic acid substrates [1].

Structural Features

Figure 1. Domain analysis of SoChABC29, the parent enzyme of SoCBM105 [2]. The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM105; 555-785 amino acids).

An AlphaFold2 [2] model predicts that SoCBM105 has a β-sandwich fold (Fig.1).

Functionalities

SoCBM105 is at the C-terminus domain of a PL29 enzyme SoChABC29 that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity [1]. Biochemical characterization of SoChABC29 and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of SoChABC29 [1].

Family Firsts

First Identified: Binding to chondroitin sulfate in the CBM105 family was first characterized and identified for SoCBM105 from the S. oris PL29 chondroitinase [1].
First Structural Characterization: No experimentally determined three-dimensional structure has been solved in this CBM family.

References

All Medline abstracts: PubMed

@@ Line 18: / Line 18: @@
 == Ligand specificities ==
-The first member of family CBM105 (SoCBM) was identified in the [[PL29]] multidomain chondroitinase ChABC29So from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while incapable of binding to other glycosaminoglycanss or polyuronic acid substrates.
+The first member of family CBM105 (SoCBM105) was identified in the [[PL29]] multidomain chondroitinase SoChABC29 from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM105 bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while it was incapable of binding to other glycosaminoglycans or polyuronic acid substrates <cite>Liu2024</cite>.
 == Structural Features ==
-[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of ChABC29So, the parent enzyme of SoCBM.''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM; 555-785 amino acids).]]
+[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of SoChABC29, the parent enzyme of SoCBM105 <cite>Jumper2021</cite>.''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM105; 555-785 amino acids).]]
-An AlphaFold2 model predicts that SoCBM has a β-sandwich fold (Fig.1).
+An AlphaFold2 <cite>Jumper2021</cite> model predicts that SoCBM105 has a β-sandwich fold (Fig.1).
 == Functionalities ==
-SoCBM is the C-terminus domain of a [[PL29]] enzyme ChABC29So that displays chondroitin sulfate ABC activity, consistent with the SoCBM specificity. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the SoCBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So.
+SoCBM105 is at the C-terminus domain of a [[PL29]] enzyme SoChABC29 that displays chondroitin sulfate ABC activity, consistent with the SoCBM105 specificity <cite>Liu2024</cite>. Biochemical characterization of SoChABC29 and the CBM-truncated enzyme revealed that the SoCBM105 enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of SoChABC29 <cite>Liu2024</cite>.
 == Family Firsts ==
-;First Identified
+;First Identified: Binding to chondroitin sulfate in the CBM105 family was first characterized and identified for SoCBM105 from the ''S. oris'' [[PL29]] chondroitinase <cite>Liu2024</cite>.
-:The chondroitin sulfate binding SoCBM from the ''S. oris'' [[PL29]] chondroitinase was the first member of the family to be identified and characterized<cite>Liu2024</cite>.
+;First Structural Characterization: No experimentally determined three-dimensional structure has been solved in this CBM family.
-;First Structural Characterization
-:No experimentally determined three-dimensional structure has been solved in this CBM family.
 == References ==
 <biblio>
 #Liu2024 pmid=38777025
+#Jumper2021 pmid=34265844
 </biblio>