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| | ==Nickel Superoxide Dismutase (NiSOD) CN-treated Apo Structure== | | ==Nickel Superoxide Dismutase (NiSOD) CN-treated Apo Structure== |
| - | <StructureSection load='1t6q' size='340' side='right' caption='[[1t6q]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='1t6q' size='340' side='right'caption='[[1t6q]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t6q]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T6Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t6q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T6Q FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t6i|1t6i]], [[1t6u|1t6u]]</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]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SODN, SOD1, SCO5254, 2SC7G11.16C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 "Actinomyces coelicolor" (Muller 1908) Lieske 1921])</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=1t6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6q OCA], [https://pdbe.org/1t6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t6q RCSB], [https://www.ebi.ac.uk/pdbsum/1t6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6q 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_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>
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| - | <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=1t6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6q OCA], [http://pdbe.org/1t6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t6q RCSB], [http://www.ebi.ac.uk/pdbsum/1t6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SODN_STRCO SODN_STRCO] |
| | == 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== |
| - | *[[Molecular Playground/Nickel Superoxide Dismutase|Molecular Playground/Nickel Superoxide Dismutase]] | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| - | *[[Superoxide Dismutase|Superoxide Dismutase]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Superoxide dismutase]] | + | [[Category: Large Structures]] |
| - | [[Category: Barondeau, D P]] | + | [[Category: Streptomyces coelicolor]] |
| - | [[Category: Bruns, C K]] | + | [[Category: Barondeau DP]] |
| - | [[Category: Getzoff, E D]] | + | [[Category: Bruns CK]] |
| - | [[Category: Kassmann, C J]] | + | [[Category: Getzoff ED]] |
| - | [[Category: Tainer, J A]] | + | [[Category: Kassmann CJ]] |
| - | [[Category: 4-helix bundle]] | + | [[Category: Tainer JA]] |
| - | [[Category: Apo]]
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| - | [[Category: Cyanide]]
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| - | [[Category: Hexamer]]
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| - | [[Category: Nickel]]
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| - | [[Category: Nisod]]
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| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sod]]
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| Structural highlights
Function
SODN_STRCO
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 1.30 A resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site. NiSOD is a hexameric assembly of right-handed 4-helix bundles of up-down-up-down topology with N-terminal hooks chelating the active site Ni ions. This newly identified nine-residue Ni-hook structural motif (His-Cys-X-X-Pro-Cys-Gly-X-Tyr) provides almost all interactions critical for metal binding and catalysis, and thus will likely be diagnostic of NiSODs. Conserved lysine residues are positioned for electrostatic guidance of the superoxide anion to the narrow active site channel. Apo structures show that the Ni-hook motif is unfolded prior to metal binding. The active site Ni geometry cycles from square planar Ni(II), with thiolate (Cys2 and Cys6) and backbone nitrogen (His1 and Cys2) ligands, to square pyramidal Ni(III) with an added axial His1 side chain ligand, consistent with electron paramagentic resonance spectroscopy. Analyses of the three NiSOD structures and comparisons to the Cu,Zn and Mn/Fe SODs support specific molecular mechanisms for NiSOD maturation and catalysis, and identify important structure-function relationships conserved among SODs.
Nickel superoxide dismutase structure and mechanism.,Barondeau DP, Kassmann CJ, Bruns CK, Tainer JA, Getzoff ED Biochemistry. 2004 Jun 29;43(25):8038-47. PMID:15209499[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Barondeau DP, Kassmann CJ, Bruns CK, Tainer JA, Getzoff ED. Nickel superoxide dismutase structure and mechanism. Biochemistry. 2004 Jun 29;43(25):8038-47. PMID:15209499 doi:10.1021/bi0496081
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