2y3u | pdb_00002y3u

CRYSTAL STRUCTURE OF APO COLLAGENASE G FROM CLOSTRIDIUM HISTOLYTICUM AT 2.55 ANGSTROM RESOLUTION

spinqualitylabelsall models 2y3u, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y3u is a 1 chain structure with sequence from "bacillus_histolyticus"_weinberg_and_seguin_1916 "bacillus histolyticus" weinberg and seguin 1916. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FLC, P6G, PEG NonStd Res: MSE Related: 2y50 Activity: Microbial collagenase, with EC number 3.4.24.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Collagen constitutes one-third of body protein in humans, reflecting its extensive role in health and disease. Of similar importance, therefore, are the idiosyncratic proteases that have evolved for collagen remodeling. The most efficient collagenases are those that enable clostridial bacteria to colonize their host tissues; but despite intense study, the structural and mechanistic basis of these enzymes has remained elusive. Here we present the crystal structure of collagenase G from Clostridium histolyticum at 2.55-A resolution. By combining the structural data with enzymatic and mutagenesis studies, we derive a conformational two-state model of bacterial collagenolysis, in which recognition and unraveling of collagen microfibrils into triple helices, as well as unwinding of the triple helices, are driven by collagenase opening and closing. Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.,Eckhard U, Schonauer E, Nuss D, Brandstetter H Nat Struct Mol Biol. 2011 Sep 25;18(10):1109-14. doi: 10.1038/nsmb.2127. PMID:21947205 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Collagenase (non-MMP)

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