Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: Evidence for decreased mobility of loops upon complexation

被引：33

作者：

Edwards, KJ

Ollis, DL

Dixon, NE

机构：

[1] Ctr. for Molec. Struct. and Function, Research School of Chemistry, Australian National University, Canberra

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1997年 / 271卷 / 02期

关键词：

peptidyl-prolyl isomerase; cyclophilin; crystal structure;

D O I：

10.1006/jmbi.1997.1151

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 Angstrom resolution. The enzyme crystallized in the orthorhombic C222(1) space group with unit cell dimensions of a = 44.7 Angstrom, b = 68.2 Angstrom and c = 102.0 Angstrom. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure. (C) Academic Press Limited.

引用

页码：258 / 265

页数：8