STRUCTURAL FEATURES OF A SUPERFAMILY OF ZINC-ENDOPEPTIDASES - THE METZINCINS

被引：168

作者：

STOCKER, W ^{[1
]}

BODE, W ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM,D-82152 MARTINSRIED,GERMANY

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1995年 / 5卷 / 03期

关键词：

D O I：

10.1016/0959-440X(95)80101-4

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：

A large number of zinc endopeptidases contain an HEXXHXXGXXH consensus motif in their catalytic site (single letter code; X is any amino acid residue). These enzymes can be grouped into four distinct families, the astacins, the adamalysins, the serralysins and the matrix metalloproteinases (matrixins). Despite a low degree of sequence similarity, their catalytic modules are topologically similar. A topology derived sequence alignment suggests that the four families form a superfamily, called the metzincins because of a perfectly superimposable methionine residue close to the zinc-binding active site. Topological similarity to the thermolysin-like enzymes indicates that these enzymes may have had a common ancestor.

引用

页码：383 / 390

页数：8

共 47 条

[11] Birkedal-Hansen, Moore, Bodden, Windsor, Birkedal-Hansen, DeCarlo, Engler, Matrix metalloproteinases: a review, Crit Rev Oral Biol Med, 4, pp. 197-250, (1993)
[12] Bode, Gomis-Ruth, Huber, Zwilling, Stocker, Structure of astacin and implications for activation of astacins and zinc ligation of collagenases, Nature, 358, pp. 164-167, (1992)
[13] Gomis-Ruth, Stocker, Huber, Zwilling, Bode, Refined 1·8 Å X-ray Crystal Structure of Astacin, a Zinc-endopeptidase from the Crayfish Astacus astacus L., Journal of Molecular Biology, 229, pp. 945-968, (1993)
[14] Gomis-Ruth, Kress, Bode, First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases., EMBO J, 12, pp. 4151-4157, (1993)
[15] Gomis-Ruth, Kress, Kellermann, Mayr, Lee, Huber, Bode, Refined 2·0 Å X-ray Crystal Structure of the Snake Venom Zinc-endopeptidase Adamalysin II, Journal of Molecular Biology, 239, pp. 513-544, (1994)
[16] Zhang, Botos, Gomis-Ruth, Doll, Blood, Njoroge, Fox, Bode, Meyer, Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase atrolysin C (form d), Proc Natl Acad Sci USA, 91, pp. 8447-8451, (1994)
[17] Baumann, Wu, Flaherty, McKay, Three-dimensional X-ray crystallographic structure of the alkaline protease of Pseudomonas aeruginosa, EMBO J, 12, pp. 3357-3364, (1993)
[18] Baumann, Crystal structure of the 50kDa metallo protease from Serratia marcescens, J Mol Biol, 242, pp. 244-251, (1994)
[19] Bode, Reinemer, Huber, Kleine, Schnierer, Tschesche, The crystal structure of human neutrophil collagenase inhibited by a substrate analog reveals the essentials for catalysis and specificity, EMBO J, 13, pp. 1263-1269, (1994)
[20] Reinemer, Grams, Huber, Kleine, Schnierer, Pieper, Tschesche, Bode, Structural implications for the role of the N-terminus in the “superactivation” of collagenases, FEBS Lett, 338, pp. 227-233, (1994)

← 1 2 3 4 5 →