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J. Biol. Chem., Vol. 283, Issue 18, 99914, May 2, 2008

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Welcome to the Carbohydrate Binding Family

Protein-carbohydrate interactions are central to numerous cellular processes, from breaking down sugars for energy to distinguishing host and pathogen. One group of proteins making such interactions possible are carbohydrate-binding modules (CBMs), ancillary proteins that are a component of multimodular enzymes that act on sugars. 50 CBM families are currently known, although this Paper of the Week by Katie Gregg and colleagues pushes that number to 51. The authors performed structural and functional studies on putative CBMs from two glycoside hydrolases of the pathogenic bacterium Clostridium perfringens. These new CBMs, GH95CBM51 and GH98CBM51, did not display much sequence similarity to existing families, but the crystal structures revealed that they formed β-sandwich folds characteristic of this class. The CBMs had differing specificity, with GH98 restricted to binding glycans bearing blood group A/B antigens whereas GH95 had a broader range, binding numerous galacto-configured sugars. Gregg and colleagues then performed a thorough bioinformatic analysis of this new family and found around 60 CBM51s that cluster into six subfamilies and include modules found in both pathogenic and non-pathogenic bacteria.

Surface representations of the binding sites of the two newly identified members of CBM family 51: GH95 (A, with bound methyl-β-D-galactose) and GH98 (D, with bound blood antigen trisaccharide).

FOOTNOTES

See referenced article, J. Biol. Chem. 2008, 283, 12604-12613

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Related Collections Papers Of The Week Social Bookmarking                      What's this?