1IAV

STRUCTURE ON NATIVE (ASN 87) SUBTILISIN FROM BACILLUS LENTUS

「1C13」から置き換えられました

1IAV の概要

• エントリーDOI: 10.2210/pdb1iav/pdb
• 分子名称: SUBTILISIN SAVINASE, SULFATE ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: subtilisins, altered flexibility, hydrolase
• 由来する生物種: Bacillus lentus
• 細胞内の位置: Secreted: P29600
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27075.81

構造登録者

Knapp, M.,Bott, R. (登録日: 2001-03-23, 公開日: 2001-04-18, 最終更新日: 2021-10-27)

主引用文献

Graycar, T.,Knapp, M.,Ganshaw, G.,Dauberman, J.,Bott, R.
Engineered Bacillus lentus subtilisins having altered flexibility.
J.Mol.Biol., 292:97-109, 1999

PubMed Abstract: The three-dimensional structures of engineered variants of Bacillus lentus subtilisin having increased enzymatic activity, K27R/N87S/V104Y/N123S/T274A (RSYSA) and N76D/N87S/S103A/V104I (DSAI), were determined by X-ray crystallography. In addition to identifying changes in atomic position we report a method that identifies protein segments having altered flexibility. The method utilizes a statistical analysis of variance to delineate main-chain temperature factors that represent significant departures from the overall variance between equivalent regions seen throughout the structure. This method reveals changes in main-chain mobility in both variants. Residues 125-127 have increased mobility in the RSYSA variant while residues 100-104 have decreased mobility in the DSAI variant. These segments are located at the substrate-binding site and changes in their mobility are believed to relate to the observed changes in proteolytic activity. The effect of altered crystal lattice contacts on segment flexibility becomes apparent when identical variants, determined in two crystal forms, are compared with the native enzyme.

PubMed: 10493860
DOI: 10.1006/jmbi.1999.3033

実験手法

X-RAY DIFFRACTION (1.8 Å)