1AH2

SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES

1AH2 の概要

• エントリーDOI: 10.2210/pdb1ah2/pdb
• 分子名称: SERINE PROTEASE PB92 (1 entity in total)
• 機能のキーワード: serine protease, subtilase, industrial enzyme, maxacal(tm), application in washing powders
• 由来する生物種: Bacillus alcalophilus
• 細胞内の位置: Secreted: P27693
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26745.41

構造登録者

Boelens, R.,Schipper, D.,Martin, J.R.,Karimi-Nejad, Y.,Mulder, F.,Zwan, J.V.D.,Mariani, M. (登録日: 1997-04-11, 公開日: 1998-04-15, 最終更新日: 2024-05-22)

主引用文献

Martin, J.R.,Mulder, F.A.,Karimi-Nejad, Y.,van der Zwan, J.,Mariani, M.,Schipper, D.,Boelens, R.
The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site.
Structure, 5:521-532, 1997

PubMed Abstract: Research on high-alkaline proteases, such as serine protease PB92, has been largely inspired by their industrial application as protein-degrading components of washing powders. Serine protease PB92 is a member of the subtilase family of enzymes, which has been extensively studied. These studies have included exhaustive protein engineering investigations and X-ray crystallography, in order to provide insight into the mechanism and specificity of enzyme catalysis. Distortions have been observed in the substrate-binding region of subtilisin crystal structures, due to crystal contacts. In addition, the structural variability in the substrate-binding region of subtilisins is often attributed to flexibility. It was hoped that the solution structure of this enzyme would provide further details about the conformation of this key region and give new insights into the functional properties of these enzymes.

PubMed: 9115441
DOI: 10.1016/S0969-2126(97)00208-6

実験手法

SOLUTION NMR