2y6t | pdb_00002y6t

Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis

spinqualitylabelsall models 2y6t, resolution 2.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y6t is a 8 chain structure with sequence from Bos taurus and Yerpy. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 2gct, 4vgc, 1gcd, 1mtn, 1gmh, 8gch, 1t8n, 1gct, 1gg6, 1t8o, 3gct, 5cha, 1p2q, 1ab9, 1gl1, 2vgc, 2cga, 1cgj, 1cho, 1cbw, 2gmt, 1ghb, 6gch, 1k2i, 1gha, 3vgc, 7gch, 3gch, 1cgi, 4gch, 1gmc, 1ca0, 1afq, 1oxg, 1gl0, 1chg, 1ggd, 2gch, 1t7c, 1yph, 1p2o, 1dlk, 1p2n, 1n8o, 1t8m, 1gmd, 4cha, 5gch, 1ex3, 1p2m, 1vgc, 1t8l, 2cha, 1hja, 6cha, 1acb Activity: Chymotrypsin, with EC number 3.4.21.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ECOT_YERPY] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases (By similarity). Publication Abstract from PubMed Resistance to antibiotics is a problem not only in terms of healthcare but also biodefense. Engineering of resistance into a human pathogen could create an untreatable biothreat pathogen. One such pathogen is Yersinia pestis, the causative agent of plague. Previously, we have used a bioinformatic approach to identify proteins that may be suitable targets for antimicrobial therapy and in particular for the treatment of plague. The serine protease inhibitor ecotin was identified as one such target. We have carried out mutational analyses in the closely related Yersinia pseudotuberculosis, validating that the ecotin gene is a virulence-associated gene in this bacterium. Y. pestis ecotin inhibits chymotrypsin. Here, we present the structure of ecotin in complex with chymotrypsin to 2.74 A resolution. The structure features a biologically relevant tetramer whereby an ecotin dimer binds to two chymotrypsin molecules, similar to what was observed in related serine protease inhibitor structures. However, the vast majority of the interactions in the present structure are distinctive, indicating that the broad specificity of the inhibitor for these proteases is based largely on its capacity to recognize features unique to each of them. These findings will have implications for the development of small ecotin inhibitors for therapeutic use. Molecular Recognition of Chymotrypsin by the Serine Protease Inhibitor Ecotin from Yersinia pestis.,Clark EA, Walker N, Ford DC, Cooper IA, Oyston PC, Acharya KR J Biol Chem. 2011 Jul 8;286(27):24015-22. Epub 2011 Apr 29. PMID:21531711 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin 3D structures Ecotin

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