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1iaa

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CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY

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

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

@@ Line 1: / Line 1: @@
-[[Image:1iaa.gif|left|200px]]<br /><applet load="1iaa" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1iaa, resolution 1.90&Aring;" />
-'''CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY'''<br />
-==Overview==
+==CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY==
-The catalytic zinc ion of astacin, a prototypical metalloproteinase from, crayfish, has been substituted by Co(II), Cu(II), Hg(II), and Ni(II) in, order to probe the role of the metal for both catalysis and structure., Compared to Zn(II)-astacin, Co(II)- and Cu(II)-astacin display enzymatic, activities of about 140 and 37%, respectively, while Ni(II)- and, Hg(II)-astacin are almost inactive. The electron paramagnetic resonance, spectrum of Cu(II)-astacin is typical of 5-fold coordinated copper(II), and its intense absorption maxima at 445 and 325 nm are probably due to, ligand-metal charge-transfer transitions involving Tyr-149. This residue, had been identified previously by x-ray crystallography of the zinc enzyme, as a zinc ligand, in addition to three imidazoles and a glutamic, acid-bound water molecule. We present now the refined high-resolution, x-ray crystal structures of Cu(II)-, Co(II)-, and Ni(II)-astacin, which, exhibit a virtually identical protein framework to the previously analyzed, structures of Zn(II)-, apo-, and Hg(II)-astacin. In Co(II)- and, Cu(II)-astacin, the metal is penta-coordinated similarly to the native, zinc enzyme. In the Ni(II) derivative, however, an additional solvent, molecule expands the metal coordination sphere to a distorted octahedral, ligand geometry, while in Hg(II)-astacin, no ordered solvent molecule at, all is observed in the inner coordination sphere of the metal. This, indicates a close correlation between catalytic properties and, ground-state metal coordination of astacin.
+<StructureSection load='1iaa' size='340' side='right'caption='[[1iaa]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1iaa]] 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=1IAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAA 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></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=1iaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iaa OCA], [https://pdbe.org/1iaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iaa RCSB], [https://www.ebi.ac.uk/pdbsum/1iaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iaa 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/1iaa_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=1iaa ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-IAA 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 CU 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAA OCA].
+*[[Proteinase 3D structures|Proteinase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structures, spectroscopic features, and catalytic properties of cobalt(II), copper(II), nickel(II), and mercury(II) derivatives of the zinc endopeptidase astacin. A correlation of structure and proteolytic activity., Gomis-Ruth FX, Grams F, Yiallouros I, Nar H, Kusthardt U, Zwilling R, Bode W, Stocker W, J Biol Chem. 1994 Jun 24;269(25):17111-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8006015 8006015]
-[[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: CU]]
-[[Category: zinc endopeptidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:12:48 2007''

1iaa

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Current revision

CRYSTAL STRUCTURES, SPECTROSCOPIC FEATURES, AND CATALYTIC PROPERTIES OF COBALT(II), COPPER(II), NICKEL(II), AND MERCURY(II) DERIVATIVES OF THE ZINC ENDOPEPTIDASE ASTACIN. A CORRELATION OF STRUCTURE AND PROTEOLYTIC ACTIVITY

Structural highlights

Function

Evolutionary Conservation

See Also

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