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spinqualitylabelsall models 1ga6, resolution 1.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (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

1GA6 is a Single protein structure of sequence from Pseudomonas sp. with CA, ACT 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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