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1ast

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Revision as of 10:33, 15 November 2017

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

Structural highlights

1ast is a 1 chain structure with sequence from Astas. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Astacin, with EC number 3.4.24.21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASTA_ASTAS] This protease prefers to cleave in front of small aliphatic residues (P1'). The presence of Lys or Arg in the P1 and P2 position yields high-turnover substrates. In the P3 position the enzyme prefers Pro > Val > Leu > Ala > Gly.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bode W, Gomis-Ruth FX, Huber R, Zwilling R, Stocker W. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature. 1992 Jul 9;358(6382):164-7. PMID:1319561 doi:http://dx.doi.org/10.1038/358164a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ast"

Categories: Astacin | Astas | Bode, W | Gomis-Rueth, F X | Stoecker, W

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF ASTACIN AND IMPLICATIONS FOR ACTIVATION OF ASTACINS AND ZINC-LIGATION OF COLLAGENASES==
 <StructureSection load='1ast' size='340' side='right' caption='[[1ast]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ast FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ast OCA], [http://pdbe.org/1ast PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ast RCSB], [http://www.ebi.ac.uk/pdbsum/1ast PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ast FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ast OCA], [http://pdbe.org/1ast PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ast RCSB], [http://www.ebi.ac.uk/pdbsum/1ast PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ast ProSAT]</span></td></tr>
 </table>
 == Function ==

1ast

From Proteopedia

Revision as of 10:33, 15 November 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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