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==ACTIVE SITE COPPER AND ZINC IONS MODULATE THE QUATERNARY STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE==
 
<StructureSection load='1oaj' size='340' side='right' caption='[[1oaj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
==Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase==
<StructureSection load='1oaj' size='340' side='right'caption='[[1oaj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oaj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OAJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oaj]] 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=1OAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAJ FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><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]] 1.73&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bzo|1bzo]], [[1ib5|1ib5]], [[1ibb|1ibb]], [[1ibd|1ibd]], [[1ibf|1ibf]], [[1ibh|1ibh]], [[1yai|1yai]], [[1oal|1oal]]</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></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=1oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaj OCA], [https://pdbe.org/1oaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oaj RCSB], [https://www.ebi.ac.uk/pdbsum/1oaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oaj ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oaj RCSB], [http://www.ebi.ac.uk/pdbsum/1oaj PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oaj_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oaj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1oaj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 recovery of the original fluorescence properties, after decompression, is fast (less than four minutes), suggesting that the isolated subunit has a relatively stable structure, and excluding the presence of stable intermediates during the dimer-monomer transition. The dimer dissociation process is still incomplete at 6.5 kbar for the copper-depleted wild-type and mutated enzymes, at variance with what is generally observed for oligomeric proteins that dissociate below 3 kbar. Measurement of the degree of dissociation, at two different protein concentrations, allows us to calculate the standard volume variation upon association, Delta V, and the dissociation constant K(d0), at atmospheric pressure, (25 ml/mol and 3 x 10(-7)M, respectively). The holoprotein is fully dimeric even at 6.5 kbar, which allows us to evaluate a lower Delta G degrees limit of 11.5 kcal/mol, corresponding to a dissociation constant K(d0)&lt;10(-9)M.
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:12595249<ref>PMID:12595249</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Superoxide Dismutase|Superoxide Dismutase]]
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Photobacterium leiognathi]]
[[Category: Large Structures]]
[[Category: Superoxide dismutase]]
[[Category: Photobacterium leiognathi subsp. leiognathi]]
[[Category: Bolognesi, M.]]
[[Category: Bolognesi M]]
[[Category: Castelli, S.]]
[[Category: Castelli S]]
[[Category: Cioni, P.]]
[[Category: Cioni P]]
[[Category: Desideri, A.]]
[[Category: Desideri A]]
[[Category: Falconi, M.]]
[[Category: Falconi M]]
[[Category: Parrilli, L.]]
[[Category: Parrilli L]]
[[Category: Pesce, A.]]
[[Category: Pesce A]]
[[Category: Rocca, B M.D.]]
[[Category: Rocca BMD]]
[[Category: Strambini, G.]]
[[Category: Strambini G]]
[[Category: Oxidoreductase]]
[[Category: Prokariotic cu]]
[[Category: Protein electrostatic]]
[[Category: Subunit interaction recognition]]
[[Category: Zn superoxide dismutase]]

Latest revision as of 11:56, 10 April 2024

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

Structural highlights

1oaj is a 1 chain structure with sequence from Photobacterium leiognathi subsp. leiognathi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.73Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SODC_PHOLE Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Evolutionary Conservation

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

See Also

1oaj, resolution 1.73Å

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