4a42 | pdb_00004a42

CpGH89CBM32-6 produced by Clostridium perfringens

spinqualitylabelsall models 4a42, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4a42 is a 2 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: CA, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8XM24_CLOPE Publication Abstract from PubMed CpGH89 is a large multimodular enzyme produced by the human and animal pathogen Clostridium perfringens. The catalytic activity of this exo-alpha-d-N-acetylglucosaminidase is directed towards a rare carbohydrate motif, N-acetyl-beta-d-glucosamine-alpha-1,4-d-galactose, which is displayed on the class III mucins deep within the gastric mucosa. In addition to the family 89 glycoside hydrolase catalytic module this enzyme has six modules that share sequence similarity to the family 32 carbohydrate-binding modules (CBM32s), suggesting the enzyme has considerable capacity to adhere to carbohydrates. Here we suggest that two of the modules, CBM32-1 and CBM32-6, are not functional as carbohydrate-binding modules (CBMs) and demonstrate that three of the CBMs, CBM32-3, CBM32-4, and CBM32-5, are indeed capable of binding carbohydrates. CBM32-3 and CBM32-4 have a novel binding specificity for N-acetyl-beta-d-glucosamine-alpha-1,4-d-galactose, which thus complements the specificity of the catalytic module. The X-ray crystal structure of CBM32-4 in complex with this disaccharide reveals a mode of recognition that is based primarily on accommodation of the unique bent shape of this sugar. In contrast, as revealed by a series of X-ray crystal structures and quantitative binding studies, CBM32-5 displays the structural and functional features of galactose binding that is commonly associated with CBM family 32. The functional CBM32s that CpGH89 contains suggest the possibility for multivalent binding events and the partitioning of this enzyme to highly specific regions within the gastrointestinal tract. Carbohydrate Recognition by an Architecturally Complex alpha-N-Acetylglucosaminidase from Clostridium perfringens.,Ficko-Blean E, Stuart CP, Suits MD, Cid M, Tessier M, Woods RJ, Boraston AB PLoS One. 2012;7(3):e33524. Epub 2012 Mar 27. PMID:22479408 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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