1ast
From Proteopedia
(New page: 200px<br /><applet load="1ast" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ast, resolution 1.8Å" /> '''STRUCTURE OF ASTACIN ...) |
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| - | [[Image:1ast.gif|left|200px]]<br /><applet load="1ast" size=" | + | [[Image:1ast.gif|left|200px]]<br /><applet load="1ast" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ast, resolution 1.8Å" /> | caption="1ast, resolution 1.8Å" /> | ||
'''STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES'''<br /> | '''STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Astacin, a digestive zinc-endopeptidase from the crayfish Astacus astacus | + | 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 Structure== | ==About this Structure== | ||
| - | 1AST is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Astacus_astacus Astacus astacus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1AST is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Astacus_astacus Astacus astacus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AST OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
| - | [[Category: Gomis-Rueth, F | + | [[Category: Gomis-Rueth, F X.]] |
[[Category: Stoecker, W.]] | [[Category: Stoecker, W.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: hydrolase(metalloproteinase)]] | [[Category: hydrolase(metalloproteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:59 2008'' |
Revision as of 09:48, 21 February 2008
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STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES
Overview
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 Structure
1AST is a Single protein structure of sequence from Astacus astacus with as ligand. Active as Astacin, with EC number 3.4.24.21 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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