1E5T

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT

1E5T の概要

• エントリーDOI: 10.2210/pdb1e5t/pdb
• 関連するPDBエントリー: 1QFM 1QFS
• 分子名称: PROLYL ENDOPEPTIDASE, GLYCEROL (3 entities in total)
• 機能のキーワード: hydrolase, prolyl oligopeptidase, amnesia, alpha/ beta-hydrolase, beta-propeller
• 由来する生物種: SUS SCROFA (PIG)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81668.18

構造登録者

Fulop, V. (登録日: 2000-08-02, 公開日: 2000-10-01, 最終更新日: 2025-10-01)

主引用文献

Fulop, V.,Szeltner, Z.,Polgar, L.
Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism
Embo Rep., 1:277-, 2000

PubMed Abstract: Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis.

PubMed: 11256612
DOI: 10.1093/EMBO-REPORTS/KVD048

実験手法

X-RAY DIFFRACTION (1.7 Å)