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| | <StructureSection load='1unf' size='340' side='right'caption='[[1unf]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='1unf' size='340' side='right'caption='[[1unf]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1unf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vigna_unguiculata Vigna unguiculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UNF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UNF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1unf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vigna_unguiculata Vigna unguiculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UNF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.97Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1unf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1unf OCA], [http://pdbe.org/1unf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1unf RCSB], [http://www.ebi.ac.uk/pdbsum/1unf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1unf ProSAT]</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=1unf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1unf OCA], [https://pdbe.org/1unf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1unf RCSB], [https://www.ebi.ac.uk/pdbsum/1unf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1unf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9M7R2_VIGUN Q9M7R2_VIGUN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] | + | [https://www.uniprot.org/uniprot/Q9M7R2_VIGUN Q9M7R2_VIGUN] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Superoxide Dismutase|Superoxide Dismutase]] | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide dismutase]] | |
| | [[Category: Vigna unguiculata]] | | [[Category: Vigna unguiculata]] |
| - | [[Category: Becana, M]] | + | [[Category: Becana M]] |
| - | [[Category: Montoya, G]] | + | [[Category: Montoya G]] |
| - | [[Category: Moran, J F]] | + | [[Category: Moran JF]] |
| - | [[Category: Munoz, I G]] | + | [[Category: Munoz IG]] |
| - | [[Category: Eukaryotic]]
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| - | [[Category: Metalloprotein]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
Q9M7R2_VIGUN Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
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
Superoxide dismutases (SODs) are a family of metalloenzymes that catalyze the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Iron superoxide dismutases (FeSODs) are only expressed in some prokaryotes and plants. A new and highly active FeSOD with an unusual subcellular localization has recently been isolated from the plant Vigna unguiculata (cowpea). This protein functions as a homodimer and, in contrast to the other members of the SOD family, is localized to the cytosol. The crystal structure of the recombinant enzyme has been solved and the model refined to 1.97 A resolution. The superoxide anion binding site is located in a cleft close to the dimer interface. The coordination geometry of the Fe site is a distorted trigonal bipyramidal arrangement, whose axial ligands are His43 and a solvent molecule, and whose in-plane ligands are His95, Asp195, and His199. A comparison of the structural features of cowpea FeSOD with those of homologous SODs reveals subtle differences in regard to the metal-protein interactions, and confirms the existence of two regions that may control the traffic of substrate and product: one located near the Fe binding site, and another in the dimer interface. The evolutionary conservation of reciprocal interactions of both monomers in neighboring active sites suggests possible subunit cooperation during catalysis.
The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis.,Munoz IG, Moran JF, Becana M, Montoya G Protein Sci. 2005 Feb;14(2):387-94. PMID:15659371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Munoz IG, Moran JF, Becana M, Montoya G. The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis. Protein Sci. 2005 Feb;14(2):387-94. PMID:15659371 doi:http://dx.doi.org/14/2/387
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