1ga4
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(New page: 200px<br /><applet load="1ga4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ga4, resolution 1.40Å" /> '''CRYSTAL STRUCTURE AN...)
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Revision as of 13:45, 20 November 2007
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CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH INHIBITOR PSEUDOIODOTYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)
Overview
The crystal structure of a pepstatin-insensitive carboxyl proteinase from, Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous, diffraction using the absorption peak of bromide anions. Structures of the, uninhibited enzyme and of complexes with an inhibitor that was either, covalently or noncovalently bound were refined at 1.0-1.4 A resolution., The structure of PSCP comprises a single compact domain with a diameter of, approximately 55 A, consisting of a seven-stranded parallel beta-sheet, flanked on both sides by a number of helices. The fold of PSCP is a, superset of the subtilisin fold, and the covalently bound inhibitor is, linked to the enzyme through a serine residue. Thus, the structure of PSCP, defines a novel family of serine-carboxyl proteinases (defined as MEROPS, S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser, 287.
About this Structure
1GA4 is a Single protein structure of sequence from Pseudomonas sp. with CA and GOL as ligands. Active as Pseudomonalisin, with EC number 3.4.21.100 Full crystallographic information is available from OCA.
Reference
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes., Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K, Nat Struct Biol. 2001 May;8(5):442-6. PMID:11323721
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