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| | <StructureSection load='3hw7' size='340' side='right'caption='[[3hw7]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3hw7' size='340' side='right'caption='[[3hw7]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hw7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HW7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3HW7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hw7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HW7 FirstGlance]. <br> |
| - | </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=CU1:COPPER+(I)+ION'>CU1</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cbj|1cbj]]</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=CU1:COPPER+(I)+ION'>CU1</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=3hw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hw7 OCA], [https://pdbe.org/3hw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hw7 RCSB], [https://www.ebi.ac.uk/pdbsum/3hw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hw7 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3hw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hw7 OCA], [http://pdbe.org/3hw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hw7 RCSB], [http://www.ebi.ac.uk/pdbsum/3hw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hw7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SODC_BOVIN SODC_BOVIN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | + | [https://www.uniprot.org/uniprot/SODC_BOVIN SODC_BOVIN] 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/hw/3hw7_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/3hw7_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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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide dismutase]]
| + | [[Category: Ascone I]] |
| - | [[Category: Ascone, I]] | + | [[Category: Savino C]] |
| - | [[Category: Savino, C]] | + | |
| - | [[Category: Antioxidant]]
| + | |
| - | [[Category: Bovine]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Flexible electrostatic loop]]
| + | |
| - | [[Category: High pressure]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
SODC_BOVIN 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 2 A resolution crystal structure of bovine erythrocyte Cu,Zn superoxide dismutase (CuZnSOD) has been determined by X-ray diffraction at high pressure (0.57 GPa) and room temperature. At 0.57 GPa the secondary, tertiary and quaternary structures are similar to other previously determined bovine erythrocyte CuZnSOD structures. Nevertheless, pressure has a localized impact on the atomic coordinates of C(alpha) atoms and on side chains. The compression of the crystal and of the protein backbone is anisotropic. This anisotropy is discussed, taking into account intermolecular contacts and protein conformation. Pressure perturbation highlights the more flexible zones in the protein such as the electrostatic loop. At 0.57 GPa, a global shift of the dimetallic sites in both subunits and changes in the oxidation state of Cu were observed. The flexibility of the electrostatic loop may be useful for the interaction of different metal carriers in the copper-uptake process, whereas the flexibility of the metal sites involved in the activity of the protein could contribute to explaining the ubiquitous character of CuZnSODs, which are found in organisms living in very different conditions, including the deep-sea environment. This work illustrates the potential of combining X-ray crystallography with high pressure to promote and stabilize higher energy conformational substates.
Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa.,Ascone I, Savino C, Kahn R, Fourme R Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):654-63. Epub 2010 May 15. PMID:20516618[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ascone I, Savino C, Kahn R, Fourme R. Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa. Acta Crystallogr D Biol Crystallogr. 2010 Jun;66(Pt 6):654-63. Epub 2010 May 15. PMID:20516618 doi:10.1107/S0907444910012321
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