1ke2

PSEUDOMONAS SERINE-CARBOXYL PROTEINASE COMPLEXED WITH THE INHIBITOR CHYMOSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)

spinqualitylabelsall models 1ke2, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ke2 is a 2 chain structure with sequence from Achromobacter georgiopolitanum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA NonStd Res: CSI, PHA Related: 1ga1, 1ga4, 1ga6, 1kdv, 1kdy, 1kdz, 1ke1 Activity: Xanthomonalisin, with EC number 3.4.21.101 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number of inhibitors, have been solved and refined at high- to atomic-level resolution. All of these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, and chymostatin, as well as previously studied iodotyrostatin and pseudo-iodotyrostatin) make covalent bonds to the active site Ser287 through their aldehyde moieties, while their side chains occupy subsites S1-S4 of the enzyme. The mode of binding of the inhibitors is almost identical for their P1 and P2 side chains, while significant differences are observed for P3 and P4 (if present). Kinetic parameters for the binding of these nanomolar inhibitors to PSCP have been established and correlated with the observed mode of binding. The preferences of this enzyme for a larger side chain in P2 as well as Tyr or Phe in P1 are explained by the size, shape, and characteristics of the S2 and S1 regions of the protein structure, respectively. Networks of hydrogen bonds involving glutamic and aspartic acids have been analyzed for the atomic-resolution structure of the native enzyme. PSCP contains a calcium-binding site that consists of Asp328, Asp348, three amide carbonyl groups, and a water molecule, in almost perfect octahedral coordination. The presence of Ca(2+) cation is necessary for the activity of the enzyme. Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase.,Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K Biochemistry. 2001 Dec 25;40(51):15602-11. PMID:11747435 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteinase

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