1GA6

CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)

Summary for 1GA6

• Entry DOI: 10.2210/pdb1ga6/pdb
• Related: 1ga1 1ga4
• Descriptor: SERINE-CARBOXYL PROTEINASE, FRAGMENT OF TYROSTATIN, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: serine-carboxyl proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Pseudomonas sp.; More
• Cellular location: Periplasm: P42790
• Total number of polymer chains: 2
• Total formula weight: 39442.22

Authors

Wlodawer, A.,Li, M.,Dauter, Z.,Gustchina, A.,Uchida, K. (deposition date: 2000-11-29, release date: 2000-12-13, Last modification date: 2024-11-13)

Primary citation

Wlodawer, A.,Li, M.,Dauter, Z.,Gustchina, A.,Uchida, K.,Oyama, H.,Dunn, B.M.,Oda, K.
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.
Nat.Struct.Biol., 8:442-446, 2001

PubMed Abstract: 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.

PubMed: 11323721
DOI: 10.1038/87610

Experimental method

X-RAY DIFFRACTION (1 Å)