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Difference between revisions of "Carbohydrate Binding Module Family 105"
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== Structural Features == | == 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 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).]] | ||
| − | An AlphaFold2 model predicts that | + | An AlphaFold2 model predicts that SoCBM105 has a β-sandwich fold (Fig.1). |
== Functionalities == | == Functionalities == | ||
Revision as of 07:33, 6 November 2024
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Ligand specificities
The first member of family CBM105 (SoCBM) was identified in the PL29 multidomain chondroitinase ChABC29So from Segatella oris [1]. SoCBM 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.
Structural Features
An AlphaFold2 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.
Family Firsts
- First Identified
- The chondroitin sulfate binding SoCBM from the S. oris PL29 chondroitinase was the first member of the family to be identified and characterized[1].
- First Structural Characterization
- No experimentally determined three-dimensional structure has been solved in this CBM family.