1P01

Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly bound peptide boronic acid

1P01 の概要

• エントリーDOI: 10.2210/pdb1p01/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000261
• 分子名称: ALPHA-LYTIC PROTEASE, N-(tert-butoxycarbonyl)-L-alanyl-N-[(1R)-1-(dihydroxyboranyl)-2-methylpropyl]-L-prolinamide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Lysobacter enzymogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20356.46

構造登録者

Bone, R.,Agard, D.A. (登録日: 1989-04-24, 公開日: 1990-04-15, 最終更新日: 2024-11-20)

主引用文献

Bone, R.,Shenvi, A.B.,Kettner, C.A.,Agard, D.A.
Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid.
Biochemistry, 26:7609-7614, 1987

PubMed Abstract: The structure of the complex formed between alpha-lytic protease, a serine protease secreted by Lysobacter enzymogenes, and N-tert-butyloxycarbonylalanylprolylvaline boronic acid (Ki = 0.35 nM) has been studied by X-ray crystallography to a resolution of 2.0 A. The active-site serine forms a covalent, nearly tetrahedral adduct with the boronic acid moiety of the inhibitor. The complex is stabilized by seven hydrogen bonds between the enzyme and inhibitor with additional stabilization arising from van der Waals interactions between enzyme and inhibitor side chains and the burying of 330 A2 of hydrophobic surface area. Hydrogen bonding between Asp-102 and His-57 remains intact in the enzyme-inhibitor complex, and His N epsilon 2 is well positioned to donate its hydrogen to the leaving group. Little change in the positions of protease residues was observed on complex formation (root mean square main chain deviation = 0.13 A), suggesting that in its native state the enzyme is complementary to tetrahedral reaction intermediates or to the nearly tetrahedral transition state for the reaction.

PubMed: 3122831
DOI: 10.1021/bi00398a012

実験手法

X-RAY DIFFRACTION (2 Å)