1GA6

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

1GA6 の概要

• エントリーDOI: 10.2210/pdb1ga6/pdb
• 関連するPDBエントリー: 1ga1 1ga4
• 分子名称: SERINE-CARBOXYL PROTEINASE, FRAGMENT OF TYROSTATIN, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: serine-carboxyl proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Pseudomonas sp.; 詳細
• 細胞内の位置: Periplasm: P42790
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39442.22

構造登録者

Wlodawer, A.,Li, M.,Dauter, Z.,Gustchina, A.,Uchida, K. (登録日: 2000-11-29, 公開日: 2000-12-13, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1 Å)