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1ast

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{{STRUCTURE_1ast| PDB=1ast | SCENE= }}
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'''STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES'''
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===STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES===
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==Overview==
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Astacin, a digestive zinc-endopeptidase from the crayfish Astacus astacus L., is the prototype for the 'astacin family', which includes mammalian metallo-endopeptidases and developmentally regulated proteins of man, fruitfly, frog and sea urchin. Here we report the X-ray crystal structure of astacin, which reveals a deep active-site cleft, with the zinc at its bottom ligated by three histidines, a water molecule and a more remote tyrosine. The third histidine (His 102) forms part of a consensus sequence, shared not only by the members of the astacin family, but also by otherwise sequentially unrelated proteinases, such as vertebrate collagenases. It may therefore represent the elusive 'third' zinc ligand in these enzymes. The amino terminus of astacin is buried forming an internal salt-bridge with Glu 103, adjacent to His 102. Astacin pro-forms extended at the N terminus, as observed for some 'latent' mammalian astacin homologues, did not exhibit this 'active' conformation, indicating an activation mechanism reminiscent of trypsin-like serine proteinases.
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{{ABSTRACT_PUBMED_1319561}}
==About this Structure==
==About this Structure==
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[[Category: Gomis-Rueth, F X.]]
[[Category: Gomis-Rueth, F X.]]
[[Category: Stoecker, W.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:31:57 2008''

Revision as of 14:32, 30 June 2008

Image:1ast.png

Template:STRUCTURE 1ast

STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES

Template:ABSTRACT PUBMED 1319561

About this Structure

1AST is a Single protein structure of sequence from Astacus astacus. Full crystallographic information is available from OCA.

Reference

Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases., Bode W, Gomis-Ruth FX, Huber R, Zwilling R, Stocker W, Nature. 1992 Jul 9;358(6382):164-7. PMID:1319561

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