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| | ==X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii== | | ==X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii== |
| - | <StructureSection load='2ji1' size='340' side='right' caption='[[2ji1]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='2ji1' size='340' side='right'caption='[[2ji1]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ji1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33931 Atcc 33931]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JI1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ji1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfarculus_baarsii Desulfarculus baarsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JI1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vzg|1vzg]], [[1vzh|1vzh]], [[1vzi|1vzi]], [[2ji2|2ji2]], [[2ji3|2ji3]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dfx, rbo, Deba_2050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=453230 ATCC 33931])</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=2ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji1 OCA], [https://pdbe.org/2ji1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ji1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ji1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ji1 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] </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=2ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji1 OCA], [http://pdbe.org/2ji1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ji1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ji1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ji1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DFX_DESB2 DFX_DESB2]] Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.<ref>PMID:10617593</ref> | + | [https://www.uniprot.org/uniprot/DFX_DESB2 DFX_DESB2] Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.<ref>PMID:10617593</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33931]] | + | [[Category: Desulfarculus baarsii]] |
| - | [[Category: Superoxide reductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Adam, V]] | + | [[Category: Adam V]] |
| - | [[Category: Amara, P]] | + | [[Category: Amara P]] |
| - | [[Category: Bourgeois, D]] | + | [[Category: Bourgeois D]] |
| - | [[Category: Carpentier, P]] | + | [[Category: Carpentier P]] |
| - | [[Category: Katona, G]] | + | [[Category: Katona G]] |
| - | [[Category: Niviere, V]] | + | [[Category: Niviere V]] |
| - | [[Category: Ohana, J]] | + | [[Category: Ohana J]] |
| - | [[Category: Tsanov, N]] | + | [[Category: Tsanov N]] |
| - | [[Category: Detoxification]]
| + | |
| - | [[Category: Electron transport]]
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| - | [[Category: Intermediate trapping]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Microspectrophotometry]]
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| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Raman spectroscopy]]
| + | |
| - | [[Category: Redox state]]
| + | |
| - | [[Category: Transport]]
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| Structural highlights
Function
DFX_DESB2 Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.[1]
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
Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.
Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.,Katona G, Carpentier P, Niviere V, Amara P, Adam V, Ohana J, Tsanov N, Bourgeois D Science. 2007 Apr 20;316(5823):449-53. PMID:17446401[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lombard M, Fontecave M, Touati D, Niviere V. Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity. J Biol Chem. 2000 Jan 7;275(1):115-21. PMID:10617593
- ↑ Katona G, Carpentier P, Niviere V, Amara P, Adam V, Ohana J, Tsanov N, Bourgeois D. Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme. Science. 2007 Apr 20;316(5823):449-53. PMID:17446401 doi:316/5823/449
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