1P10

STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES

1P10 の概要

• エントリーDOI: 10.2210/pdb1p10/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000316
• 分子名称: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-VALINE BORONIC ACID INHIBITOR, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: serine proteinase, 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: 2
• 化学式量合計: 20381.40

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: 2024-06-05)

主引用文献

Bone, R.,Silen, J.L.,Agard, D.A.
Structural plasticity broadens the specificity of an engineered protease.
Nature, 339:191-195, 1989

PubMed Abstract: The substrate specificity of alpha-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met with Ala. The substrate specificity of both this mutant and another similar mutant are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, a combination of alternate side-chain conformations and binding-site flexibility, allows both large and small substrates to be well accommodated.

PubMed: 2716847
DOI: 10.1038/339191a0

実験手法

X-RAY DIFFRACTION (2.25 Å)