1LW6

Crystal Structure of the Complex of Subtilisin BPN' with Chymotrypsin Inhibitor 2 at 1.5 Angstrom Resolution

1LW6 の概要

• エントリーDOI: 10.2210/pdb1lw6/pdb
• 分子名称: SUBTILISIN BPN', SUBTILISIN-CHYMOTRYPSIN INHIBITOR-2A, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: serine protease, inhibitor, hydrolase
• 由来する生物種: Bacillus amyloliquefaciens; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36061.31

構造登録者

Radisky, E.S.,Koshland JR., D.E. (登録日: 2002-05-30, 公開日: 2002-08-21, 最終更新日: 2024-02-14)

主引用文献

Radisky, E.S.,Koshland Jr., D.E.
A clogged gutter mechanism for protease inhibitors.
Proc.Natl.Acad.Sci.USA, 99:10316-10321, 2002

PubMed Abstract: A classical peptide inhibitor of serine proteases that is hydrolyzed approximately 10(7) times more slowly than a good substrate is shown to form an acyl-enzyme intermediate rapidly. Despite this quick first step, further reaction is slowed dramatically because of tight and oriented binding of the cleaved peptide, preventing acyl-enzyme hydrolysis and favoring the reverse reaction. Moreover, this mechanism appears to be common to a large class of tight-binding serine protease inhibitors that mimic good substrates. The arrest of enzymatic reaction at the intermediate stage allowed us to determine that the consensus nucleophilic attack angle is close to 90 degrees in the reactive Michaelis complexes.

PubMed: 12142461
DOI: 10.1073/pnas.112332899

実験手法

X-RAY DIFFRACTION (1.5 Å)