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1iad

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REFINED 1.8 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF ASTACIN, A ZINC-ENDOPEPTIDASE FROM THE CRAYFISH ASTACUS ASTACUS L. STRUCTURE DETERMINATION, REFINEMENT, MOLECULAR STRUCTURE AND COMPARISON TO THERMOLYSIN

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

Categories: Astacus astacus | Large Structures | Bode W | Gomis-Rueth F-X | Stoecker W

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-[[Image:1iad.gif|left|200px]]<br /><applet load="1iad" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1iad, resolution 2.3&Aring;" />
-'''REFINED 1.8 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF ASTACIN, A ZINC-ENDOPEPTIDASE FROM THE CRAYFISH ASTACUS ASTACUS L. STRUCTURE DETERMINATION, REFINEMENT, MOLECULAR STRUCTURE AND COMPARISON TO THERMOLYSIN'''<br />
-==Overview==
+==REFINED 1.8 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF ASTACIN, A ZINC-ENDOPEPTIDASE FROM THE CRAYFISH ASTACUS ASTACUS L. STRUCTURE DETERMINATION, REFINEMENT, MOLECULAR STRUCTURE AND COMPARISON TO THERMOLYSIN==
-Astacin, a 200 residue digestive zinc-endopeptidase from the crayfish, Astacus astacus L., is the prototype of the "astacin family", which, comprises several membrane-bound mammalian endopeptidases and, developmentally implicated regulatory proteins. Large trigonal crystals of, astacin were grown, and X-ray reflection data to 1.8 A resolution were, collected. The astacin structure has been solved by multiple isomorphous, replacement using six heavy-atom derivatives, and refined to a, crystallographic R-value of 0.158 applying stringent constraints. All 200, residues are clearly defined by electron density; 181 solvent molecules, have been localized. Besides the native structure, the structures of, Hg-astacin (with a mercury ion replacing the zinc) and of the apoenzyme, were also refined. The astacin molecule exhibits a kidney-like shape. It, consists of an amino-terminal and a carboxy-terminal domain, with a deep, active-site cleft in between. The zinc ion, located at the bottom of this, cleft, is co-ordinated in a novel trigonal-bipyramidal geometry by three, histidine residues, a tyrosine and by a water molecule, which is also, bound to the carboxylate side-chain of Glu93. The amino-terminal domain of, astacin consists mainly of two long alpha-helices, one centrally located, and one more peripheral, and of a five-stranded pleated beta-sheet. The, amino terminus protrudes into an internal, water-filled cavity of the, lower domain and forms a buried salt bridge with Glu103; amino-terminally, extended pro-forms of astacin are thus not compatible with this structure., The carboxy-terminal domain of astacin is mainly organized in several, turns and irregular structures. Because they share sequence identity of, about 35%, the structures of the proteolytic domains of the other, "astacin" members must be quite similar to astacin. Only a few very short, deletions and insertions quite distant from the active-site distinguish, their structures from astacin. The five-stranded beta-sheet and the two, helices of the amino-terminal domain of astacin are topologically similar, to the structure observed in the archetypal zinc-endopeptidase, thermolysin; the rest of the structures are, in contrast, completely, unrelated in astacin and thermolysin. The zinc ion, the central, alpha-helix and the zinc-liganding residues His92, Glu93 and His96 of, astacin are nearly superimposable with the respective groups of, thermolysin, namely with the zinc ion, the "active-site helix", and, His142TL, Glu143TL and His146TL of the zinc-binding consensus motif, His-Glu-Xaa-Xaa-His (where Xaa is any amino acid residue).(ABSTRACT, TRUNCATED AT 400 WORDS)
+<StructureSection load='1iad' size='340' side='right'caption='[[1iad]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1iad]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Astacus_astacus Astacus astacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iad OCA], [https://pdbe.org/1iad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iad RCSB], [https://www.ebi.ac.uk/pdbsum/1iad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iad ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ASTA_ASTAS 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ia/1iad_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iad ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-IAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Astacus_astacus Astacus astacus]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAD OCA].
+*[[Proteinase 3D structures|Proteinase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin., Gomis-Ruth FX, Stocker W, Huber R, Zwilling R, Bode W, J Mol Biol. 1993 Feb 20;229(4):945-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8445658 8445658]
-[[Category: Astacin]]
 [[Category: Astacus astacus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bode, W.]]
+[[Category: Bode W]]
-[[Category: Gomis-Rueth, F.X.]]
+[[Category: Gomis-Rueth F-X]]
-[[Category: Stoecker, W.]]
+[[Category: Stoecker W]]
-[[Category: zinc endopeptidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:12:58 2007''

1iad

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REFINED 1.8 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF ASTACIN, A ZINC-ENDOPEPTIDASE FROM THE CRAYFISH ASTACUS ASTACUS L. STRUCTURE DETERMINATION, REFINEMENT, MOLECULAR STRUCTURE AND COMPARISON TO THERMOLYSIN

Structural highlights

Function

Evolutionary Conservation

See Also

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