2j7m | pdb_00002j7m

CHARACTERIZATION OF A FAMILY 32 CBM

spinqualitylabelsall models 2j7m, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2j7m is a 1 chain structure with sequence from "bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898. This structure supersedes the now removed PDB entry 2j1f. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FUC, GAL, NDG Related: 2cbi, 2cbj, 2j1a, 2j1e Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Clostridium perfringens is a notable colonizer of the human gastrointestinal tract. This bacterium is quite remarkable for a human pathogen by the number of glycoside hydrolases found in its genome. The modularity of these enzymes is striking as is the frequent occurrence of modules having amino acid sequence identity with family 32 carbohydrate-binding modules (CBMs), often referred to as F5/8 domains. Here we report the properties of family 32 CBMs from a C. perfringens N-acetyl-beta-hexosaminidase. Macroarray, UV difference, and isothermal titration calorimetry binding studies indicate a preference for the disaccharide LacNAc (beta-d-galactosyl-1,4-beta-d-N-acetylglucosamine). The molecular details of the interaction of this CBM with galactose, LacNAc, and the type II blood group H-trisaccharide are revealed by x-ray crystallographic studies at resolutions of 1.49, 2.4, and 2.3 A, respectively. The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor.,Ficko-Blean E, Boraston AB J Biol Chem. 2006 Dec 8;281(49):37748-57. Epub 2006 Sep 21. PMID:16990278 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hyaluronidase

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