1.56-ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE

被引：183

作者：

SPURLINO, JC ^{[1
]}

SMALLWOOD, AM ^{[1
]}

CARLTON, DD ^{[1
]}

BANKS, TM ^{[1
]}

VAVRA, KJ ^{[1
]}

JOHNSON, JS ^{[1
]}

COOK, ER ^{[1
]}

FALVO, J ^{[1
]}

WAHL, RC ^{[1
]}

PULVINO, TA ^{[1
]}

WENDOLOSKI, JJ ^{[1
]}

SMITH, DL ^{[1
]}

机构：

[1] EASTMAN KODAK CO,ROCHESTER,NY 14650

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1994年 / 19卷 / 02期

关键词：

CRYSTALLOGRAPHY; HYDROXAMATE; HIGH RESOLUTION; METALLOPROTEINASE; ZINC; X-RAY;

D O I：

10.1002/prot.340190203

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 X-ray crystal structure of a 19 kDa active fragment of human fibroblast collagenase has been determined by the multiple isomorphous replacement method and refined at 1.56 Angstrom resolution to an R-factor of 17.4%. The current structure includes a bound hydroxamate inhibitor, 88 waters and three metal atoms (two zincs and a calcium). The overall topology of the enzyme, comprised of a five stranded beta-sheet and three alpha-helices, is similar to the thermolysin-like metalloproteinases. There are some important differences between the collagenase and thermolysin families of enzymes. The active site zinc ligands are all histidines (His-218, His-222, and His-228). The presence of a second zinc ion in a structural role is a unique feature of the matrix metalloproteinases. The binding properties of the active site cleft are more dependent on the main chain conformation of the enzyme (and substrate) compared with thermolysin. A mechanism of action for peptide cleavage similar to that of thermolysin is proposed for fibroblast collagenase. (C) 1994 Wiley-Liss, Inc.

引用

页码：98 / 109

页数：12

共 28 条

[1] PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].