NDLI: Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.

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Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Abbott, D. Wade Boraston, Alisdair B. Finn, Ron Gregg, Katie J.
Description	Author Affiliation: Gregg KJ ( Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.)
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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	18
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-05-02
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carbohydrate Metabolism Clostridium Perfringens Enzymology Glycoside Hydrolases Chemistry Amino Acid Sequence Binding Sites Blood Group Antigens Calcium Metabolism Crystallography, X-Ray Galactose Genetic Variation Models, Molecular Molecular Sequence Data Protein Structure, Secondary Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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