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PMID: 7663339 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.

Protein science : a publication of the Protein Society ·Vol. 4 ·No. 5 ·1995-05-00 ·Pages 823-40

Stöcker W, Grams F, Baumann U, Reinemer P, Gomis-Rüth FX, McKay DB, Bode W

Abstract

The three-dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin II from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from crayfish are topologically similar, with respect to a five-stranded beta-sheet and three alpha-helices arranged in typical sequential order. The four proteins exhibit the characteristic consensus motif HEXXHXXGXXH, whose three histidine residues are involved in binding of the catalytically essential zinc ion. Moreover, they all share a conserved methionine residue beneath the active site metal as part of a superimposable "Met-turn." This structural relationship is supported by a sequence alignment performed on the basis of topological equivalence showing faint but distinct sequential similarity. The alkaline proteinase is about equally distant (26% sequence identity) to both human neutrophil collagenase and astacin and a little further away from adamalysin II (17% identity). The pairs astacin/adamalysin II, astacin/human neutrophil collagenase, and adamalysin II/human neutrophil collagenase exhibit sequence identities of 16%, 14%, and 13%, respectively. Therefore, the corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins/reprolysins (snake venom proteinases/reproductive tract proteins), and the serralysins (large bacterial proteases from Serratia, Erwinia, and Pseudomonas) appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation "metzincins" has been proposed. There is also a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, which share the truncated zinc-binding motif HEXXH and, moreover, similar topologies in their N-terminal domains.

MeSH Terms
Amino Acid Sequence Binding Sites Biological Evolution Collagenases/chemistry,metabolism Matrix Metalloproteinase 8 Metalloendopeptidases/chemistry,metabolism Molecular Sequence Data Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Serine Endopeptidases/chemistry,metabolism
Chemicals
Pseudomonas serine proteinase Serine Endopeptidases Collagenases Metalloendopeptidases astacin Matrix Metalloproteinase 8 Crotalus adamanteus proteinase II
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Stöcker W
Zoologisches Institut, Universität Heidelberg, Germany.
Grams F
Baumann U
Reinemer P
Gomis-Rüth F X
McKay D B
Bode W
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
DOI
10.1002/pro.5560040502
Published
1995-05-00
Pages
823-40
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2143131
Subset
IM
External Links
PubMed source DOI: 10.1002/pro.5560040502 PMC Full Text View journal details
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