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

共 32 条

[1]

BRUNGER AT, 1992, XPLOR VERSION 3 1 SY

[2] N-15 NMR RELAXATION STUDIES OF THE FK506 BINDING-PROTEIN - DYNAMIC EFFECTS OF LIGAND-BINDING AND IMPLICATIONS FOR CALCINEURIN RECOGNITION [J].

CHENG, JW ;

LEPRE, CA ;

MOORE, JM .

BIOCHEMISTRY, 1994, 33 (14) :4093-4100

[3] 3-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA-COLI PERIPLASMIC CYCLOPHILIN [J].

CLUBB, RT ;

FERGUSON, SB ;

WALSH, CT ;

WAGNER, G .

BIOCHEMISTRY, 1994, 33 (10) :2761-2772

[4] STRUCTURAL AND FUNCTIONAL-CHARACTERIZATION OF ESCHERICHIA-COLI PEPTIDYL-PROLYL CIS-TRANS-ISOMERASES [J].

COMPTON, LA ;

DAVIS, JM ;

MACDONALD, JR ;

BACHINGER, HP .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 206 (03) :927-934

[5] THE MUTANT ESCHERICHIA-COLI F112W CYCLOPHILIN BINDS CYCLOSPORINE-A IN NEARLY IDENTICAL CONFORMATION AS HUMAN CYCLOPHILIN [J].

FEJZO, J ;

ETZKORN, FA ;

CLUBB, RT ;

SHI, Y ;

WALSH, CT ;

WAGNER, G .

BIOCHEMISTRY, 1994, 33 (19) :5711-5720

[6] CYCLOPHILIN AND PEPTIDYL-PROLYL CIS-TRANS ISOMERASE ARE PROBABLY IDENTICAL PROTEINS [J].

FISCHER, G ;

WITTMANNLIEBOLD, B ;

LANG, K ;

KIEFHABER, T ;

SCHMID, FX .

NATURE, 1989, 337 (6206) :476-478

[7] PEPTIDYLPROLINE CIS-TRANS-ISOMERASES - IMMUNOPHILINS [J].

GALAT, A .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 216 (03) :689-707

[8] 2 DISTINCT FORMS OF PEPTIDYLPROLYL-CIS-TRANS-ISOMERASE ARE EXPRESSED SEPARATELY IN PERIPLASMIC AND CYTOPLASMIC COMPARTMENTS OF ESCHERICHIA-COLI-CELLS [J].

HAYANO, T ;

TAKAHASHI, N ;

KATO, S ;

MAKI, N ;

SUZUKI, M .

BIOCHEMISTRY, 1991, 30 (12) :3041-3048

[9] DICTIONARY OF PROTEIN SECONDARY STRUCTURE - PATTERN-RECOGNITION OF HYDROGEN-BONDED AND GEOMETRICAL FEATURES [J].

KABSCH, W ;

SANDER, C .

BIOPOLYMERS, 1983, 22 (12) :2577-2637

[10] THE X-RAY STRUCTURE OF A TETRAPEPTIDE BOUND TO THE ACTIVE-SITE OF HUMAN CYCLOPHILIN-A [J].

KALLEN, J ;

WALKINSHAW, MD .

FEBS LETTERS, 1992, 300 (03) :286-290

← 1 2 3 4 →