2AGI

The leupeptin-trypsin covalent complex at 1.14 A resolution

2AGI の概要

• エントリーDOI: 10.2210/pdb2agi/pdb
• 関連するPDBエントリー: 2AGE 2AGG 2AH4
• 関連するBIRD辞書のPRD_ID: PRD_000216
• 分子名称: beta-trypsin, leupeptin, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: acyl-enzyme, serine protease, proteinase, peptidase, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00760
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23986.07

構造登録者

Radisky, E.S.,Lee, J.M.,Lu, C.J.,Koshland Jr., D.E. (登録日: 2005-07-26, 公開日: 2006-05-16, 最終更新日: 2024-11-06)

主引用文献

Radisky, E.S.,Lee, J.M.,Lu, C.J.,Koshland Jr., D.E.
Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates
Proc.Natl.Acad.Sci.USA, 103:6835-6840, 2006

PubMed Abstract: Atomic resolution structures of trypsin acyl-enzymes and a tetrahedral intermediate analog, along with previously solved structures representing the Michaelis complex, are used to reconstruct events in the catalytic cycle of this classic serine protease. Structural comparisons provide insight into active site adjustments involved in catalysis. Subtle motions of the catalytic serine and histidine residues coordinated with translation of the substrate reaction center are seen to favor the forward progress of the acylation reaction. The structures also clarify the attack trajectory of the hydrolytic water in the deacylation reaction.

PubMed: 16636277
DOI: 10.1073/pnas.0601910103

実験手法

X-RAY DIFFRACTION (1.14 Å)