1ast: Difference between revisions

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[[Image:1ast.gif|left|200px]]
[[Image:1ast.gif|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Astacin Astacin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.21 3.4.24.21] </span>
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'''STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES'''
'''STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES'''
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[[Category: Gomis-Rueth, F X.]]
[[Category: Gomis-Rueth, F X.]]
[[Category: Stoecker, W.]]
[[Category: Stoecker, W.]]
[[Category: hydrolase(metalloproteinase)]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:39:19 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:46:50 2008''

Revision as of 10:39, 2 May 2008

File:1ast.gif

Template:STRUCTURE 1ast

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


OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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 Page seeded by OCA on Fri May 2 10:39:19 2008

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