2VNO

Family 51 carbohydrate binding module from a family 98 glycoside hydrolase produced by Clostridium perfringens in complex with blood group B-trisaccharide ligand.

Summary for 2VNO

• Entry DOI: 10.2210/pdb2vno/pdb
• Related: 2VNG 2VNR
• Descriptor: CPE0329, alpha-L-fucopyranose-(1-2)-[beta-D-galactopyranose-(1-3)]beta-D-galactopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: family 51 carbohydrate binding module, clostridium perfringens, family 98 glycoside hydrolase, b-trisaccharide, blood group antigens, hydrolase
• Biological source: CLOSTRIDIUM PERFRINGENS
• Total number of polymer chains: 2
• Total formula weight: 40807.12

Authors

Gregg, K.J.,Finn, R.,Abbott, D.W.,Boraston, A.B. (deposition date: 2008-02-05, release date: 2008-02-19, Last modification date: 2024-05-08)

Primary citation

Gregg, K.J.,Finn, R.,Abbott, D.W.,Boraston, A.B.
Divergent Modes of Glycan Recognition by a New Family of Carbohydrate-Binding Modules
J.Biol.Chem., 283:12604-, 2008

PubMed Abstract: The genomes of myonecrotic Clostridium perfringens isolates contain genes encoding a large and fascinating array of highly modular glycoside hydrolase enzymes. Although the catalytic activities of many of these enzymes are somewhat predictable based on their amino acid sequences, the functions of their abundant ancillary modules are not and remain poorly studied. Here, we present the structural and functional analysis of a new family of ancillary carbohydrate-binding modules (CBMs), CBM51, which was previously annotated in data bases as the novel putative CBM domain. The high resolution crystal structures of two CBM51 members, GH95CBM51 and GH98CBM51, from a putative family 95 alpha-fucosidase and from a family 98 blood group A/B antigen-specific endo-beta-galactosidase, respectively, showed them to have highly similar beta-sandwich folds. However, GH95CBM51 was shown by glycan microarray screening, isothermal titration calorimetry, and x-ray crystallography to bind galactose residues, whereas the same analyses of GH98CBM51 revealed specificity for the blood group A/B antigens through non-conserved interactions. Overall, this work identifies a new family of CBMs with many members having apparent specificity for eukaryotic glycans, in keeping with the glycan-rich environment C. perfringens would experience in its host. However, a wider bioinformatic analysis of this CBM family also indicated a large number of members in non-pathogenic environmental bacteria, suggesting a role in the recognition of environmental glycans.

PubMed: 18292090
DOI: 10.1074/JBC.M709865200

Experimental method

X-RAY DIFFRACTION (1.45 Å)