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’

FEBS Letters

Gomis-Rüth, Franz-Xaver³  Bode, Wolfram²  Stöckler, Walter¹ 

[1] Zoologisches Institut der Universität Heidelberg, Fachrichtung Physiologie, 69120 Heidelberg, Germany;Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, 82152 Martinsried (bei München, Germany;Institut de Biologia Fonamental, Universität Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain

关键词: Astacin: Snake venom metalloproteinase;    Matrix metalloproteinase;    Thermolysin;    Zinc endopeptidase family;    Protein crystal structure;   

DOI  :  10.1016/0014-5793(93)80312-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown