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| | ==Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase== | | ==Active site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase== |
| - | <StructureSection load='1oal' size='340' side='right' caption='[[1oal]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='1oal' size='340' side='right'caption='[[1oal]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1oal]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"photobacterium_leiognathi_subsp._leiognathi"_(boisvert_et_al._1967)_ast_and_dunlap_2004 "photobacterium leiognathi subsp. leiognathi" (boisvert et al. 1967) ast and dunlap 2004]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OAL FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bzo|1bzo]], [[1ib5|1ib5]], [[1ibb|1ibb]], [[1ibd|1ibd]], [[1ibf|1ibf]], [[1ibh|1ibh]], [[1oaj|1oaj]], [[1yai|1yai]]</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 id='activity'><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=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> |
| - | <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=1oal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oal OCA], [http://pdbe.org/1oal PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oal RCSB], [http://www.ebi.ac.uk/pdbsum/1oal PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oal ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SODC_PHOLE SODC_PHOLE]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | + | [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]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oal_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oal_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1oal" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1oal" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Superoxide dismutase]] | + | [[Category: Large Structures]] |
| - | [[Category: Bolognesi, M]] | + | [[Category: Photobacterium leiognathi subsp. leiognathi]] |
| - | [[Category: Castellifalconiparrilli, L]] | + | [[Category: Bolognesi M]] |
| - | [[Category: Cioni, P]] | + | [[Category: Castellifalconiparrilli L]] |
| - | [[Category: Desideri, A]] | + | [[Category: Cioni P]] |
| - | [[Category: Pesce, A]] | + | [[Category: Desideri A]] |
| - | [[Category: Rocca, B M.D]] | + | [[Category: Pesce A]] |
| - | [[Category: Strambini, G]] | + | [[Category: Rocca BMD]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Strambini G]] |
| - | [[Category: Prokaryotic cu]]
| + | |
| - | [[Category: Protein electrostatic]]
| + | |
| - | [[Category: Protein-subunit interaction recognition]]
| + | |
| - | [[Category: Zn superoxide dismutase]]
| + | |
| Structural highlights
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.
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)<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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cioni P, Pesce A, Morozzo della Rocca B, Castelli S, Falconi M, Parrilli L, Bolognesi M, Strambini G, Desideri A. Active-site copper and zinc ions modulate the quaternary structure of prokaryotic Cu,Zn superoxide dismutase. J Mol Biol. 2003 Mar 7;326(5):1351-60. PMID:12595249
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