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| <StructureSection load='1yai' size='340' side='right'caption='[[1yai]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1yai' size='340' side='right'caption='[[1yai]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1yai]] is a 3 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=1YAI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YAI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yai]] is a 3 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=1YAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YAI 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=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]] 1.9Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHSOD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=658 "Photobacterium leiognathi subsp. leiognathi" (Boisvert et al. 1967) Ast and Dunlap 2004])</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=1yai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yai OCA], [https://pdbe.org/1yai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yai RCSB], [https://www.ebi.ac.uk/pdbsum/1yai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yai 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=1yai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yai OCA], [http://pdbe.org/1yai PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yai RCSB], [http://www.ebi.ac.uk/pdbsum/1yai PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yai 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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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Superoxide dismutase]] | + | [[Category: Photobacterium leiognathi subsp. leiognathi]] |
- | [[Category: Bourne, Y]] | + | [[Category: Bourne Y]] |
- | [[Category: Getzoff, E D]] | + | [[Category: Getzoff ED]] |
- | [[Category: Lo, T P]] | + | [[Category: Lo TP]] |
- | [[Category: Redford, S M]] | + | [[Category: Redford SM]] |
- | [[Category: Tainer, J A]] | + | [[Category: Tainer JA]] |
- | [[Category: Beta-barrel]]
| + | |
- | [[Category: Macromolecular assembly]]
| + | |
- | [[Category: Metalloenzyme]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
| 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
Eukaryotic Cu,Zn superoxide dismutases (CuZnSODs) are antioxidant enzymes remarkable for their unusually stable beta-barrel fold and dimer assembly, diffusion-limited catalysis, and electrostatic guidance of their free radical substrate. Point mutations of CuZnSOD cause the fatal human neurodegenerative disease amyotrophic lateral sclerosis. We determined and analyzed the first crystallographic structure (to our knowledge) for CuZnSOD from a prokaryote, Photobacterium leiognathi, a luminescent symbiont of Leiognathid fish. This structure, exemplifying prokaryotic CuZnSODs, shares the active-site ligand geometry and the topology of the Greek key beta-barrel common to the eukaryotic CuZnSODs. However, the beta-barrel elements recruited to form the dimer interface, the strategy used to forge the channel for electrostatic recognition of superoxide radical, and the connectivity of the intrasubunit disulfide bond in P. leiognathi CuZnSOD are discrete and strikingly dissimilar from those highly conserved in eukaryotic CuZnSODs. This new CuZnSOD structure broadens our understanding of structural features necessary and sufficient for CuZnSOD activity, highlights a hitherto unrecognized adaptability of the Greek key beta-barrel building block in evolution, and reveals that prokaryotic and eukaryotic enzymes diverged from one primordial CuZnSOD and then converged to distinct dimeric enzymes with electrostatic substrate guidance.
Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase.,Bourne Y, Redford SM, Steinman HM, Lepock JR, Tainer JA, Getzoff ED Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12774-9. PMID:8917495[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bourne Y, Redford SM, Steinman HM, Lepock JR, Tainer JA, Getzoff ED. Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase. Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12774-9. PMID:8917495
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