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1oal

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(New page: 200px<br /> <applet load="1oal" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oal, resolution 1.50&Aring;" /> '''ACTIVE SITE COPPER ...)
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[[Image:1oal.gif|left|200px]]<br />
 
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<applet load="1oal" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oal, resolution 1.50&Aring;" />
 
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'''ACTIVE SITE COPPER AND ZINC IONS MODULATE THE QUATERNARY STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE'''<br />
 
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==Overview==
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==Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase==
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The influence of the constitutive metal ions on the equilibrium properties, of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase has been, studied for the wild-type and for two mutant protein forms bearing a, negative charge in the amino acid clusters at the dimer association, interface. Depletion of copper and zinc dissociates the two mutant, proteins into monomers, which reassemble toward the dimeric state upon, addition of stoichiometric amounts of zinc. Pressure-dependent, dissociation is observed for the copper-depleted wild-type and mutated, enzymes, as monitored by the fluorescence shift of a unique tryptophan, residue located at the subunit association interface. The spectral shift, occurs slowly, reaching a plateau after 15-20 minutes, and is fully, reversible. The ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12595249 (full description)]]
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<StructureSection load='1oal' size='340' side='right'caption='[[1oal]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oal]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_leiognathi_subsp._leiognathi Photobacterium leiognathi subsp. leiognathi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oal OCA], [https://pdbe.org/1oal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oal RCSB], [https://www.ebi.ac.uk/pdbsum/1oal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oal ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SODC_PHOLE SODC_PHOLE] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oal_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1oal ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1OAL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi]] with ZN and CU as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAL OCA]].
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase., Cioni P, Pesce A, Morozzo della Rocca B, Castelli S, Falconi M, Parrilli L, Bolognesi M, Strambini G, Desideri A, J Mol Biol. 2003 Mar 7;326(5):1351-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595249 12595249]
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[[Category: Large Structures]]
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[[Category: Photobacterium leiognathi]]
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[[Category: Photobacterium leiognathi subsp. leiognathi]]
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[[Category: Single protein]]
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[[Category: Bolognesi M]]
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[[Category: Bolognesi, M.]]
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[[Category: Castellifalconiparrilli L]]
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[[Category: Castellifalconiparrilli, L.]]
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[[Category: Cioni P]]
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[[Category: Cioni, P.]]
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[[Category: Desideri A]]
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[[Category: Desideri, A.]]
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[[Category: Pesce A]]
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[[Category: Pesce, A.]]
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[[Category: Rocca BMD]]
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[[Category: Rocca, B.M.D.]]
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[[Category: Strambini G]]
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[[Category: Strambini, G.]]
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[[Category: CU]]
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[[Category: ZN]]
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[[Category: oxidoreductase]]
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[[Category: prokaryotic cu]]
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[[Category: protein electrostatic]]
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[[Category: protein-subunit interaction recognition]]
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[[Category: zn superoxide dismutase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:53:47 2007''
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Current revision

Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase

PDB ID 1oal

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