Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'.
The X-ray crystal structures of two zinc endopeptidases, astacin from crayfish, and adamalysin II from snake venom, reveal a strong overall topological equivalence and virtually identical extended HEXXHXXGXXH zinc-binding segments, but in addition a methionine-containing turn of similar conformation (the 'Met-turn'), which forms a hydrophobic basis for the zinc ion and the three liganding histidine residues. These two features are also present in a similar arrangement in the matrix metalloproteinases (matrixins) and in the large bacterial Serratia proteinase-like peptidases (serralysins). We suggest that these four proteinases represent members of distinct subfamilies which can be grouped together in a family, for which we propose the designation, metzincins.
Bode
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Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried (bei München), Germany.
Gomis-Rüth
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FX
Stöckler
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D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry* / Q000145:classification; D005109:Extracellular Matrix / Q000201:enzymology; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000145:classification; D008715:Methionine / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012705:Serratia / Q000201:enzymology; D012910:Snake Venoms / Q000737:chemistry* / Q000145:classification; D015032:Zinc / Q000737:chemistry*
D012910:Snake Venoms; D008715:Methionine; D010450:Endopeptidases; D008666:Metalloendopeptidases; C071288:astacin; D015032:Zinc