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| | <StructureSection load='4x9q' size='340' side='right'caption='[[4x9q]], [[Resolution|resolution]] 1.77Å' scene=''> | | <StructureSection load='4x9q' size='340' side='right'caption='[[4x9q]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4x9q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X9Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4x9q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X9Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sod-3, C08A9.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4x9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9q OCA], [https://pdbe.org/4x9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x9q RCSB], [https://www.ebi.ac.uk/pdbsum/4x9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9q 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>
| + | |
| - | <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=4x9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9q OCA], [http://pdbe.org/4x9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x9q RCSB], [http://www.ebi.ac.uk/pdbsum/4x9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SODM2_CAEEL SODM2_CAEEL]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | + | [https://www.uniprot.org/uniprot/SODM2_CAEEL SODM2_CAEEL] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Superoxide Dismutase|Superoxide Dismutase]] | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide dismutase]]
| + | [[Category: Bonetta R]] |
| - | [[Category: Bonetta, R]] | + | [[Category: Hunter GJ]] |
| - | [[Category: Hunter, G J]] | + | [[Category: Hunter T]] |
| - | [[Category: Hunter, T]] | + | [[Category: Stewart EE]] |
| - | [[Category: Stewart, E E]] | + | [[Category: Trinh CH]] |
| - | [[Category: Trinh, C H]] | + | |
| - | [[Category: Dismutase]]
| + | |
| - | [[Category: Manganese]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Superoxide]]
| + | |
| Structural highlights
Function
SODM2_CAEEL Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Publication Abstract from PubMed
C. elegans MnSOD-3 has been implicated in the longevity pathway and its mechanism of catalysis is relevant to the aging process and carcinogenesis. The structures of MnSOD-3 provide unique crystallographic evidence of a dynamic region of the tetrameric interface (residues 41-54). We have determined the structure of the MnSOD-3-azide complex to 1.77-A resolution. Analysis of this complex shows that the substrate analog, azide, binds end-on to the manganese center as a sixth ligand and that it ligates directly to a third and new solvent molecule also positioned within interacting distance to the His30 and Tyr34 residues of the substrate access funnel. This is the first structure of a eukaryotic MnSOD-azide complex that demonstrates the extended, uninterrupted hydrogen-bonded network that forms a proton relay incorporating three outer sphere solvent molecules, the substrate analog, the gateway residues, Gln142, and the solvent ligand. This configuration supports the formation and release of the hydrogen peroxide product in agreement with the 5-6-5 catalytic mechanism for MnSOD. The high product dissociation constant k4 of MnSOD-3 reflects low product inhibition making this enzyme efficient even at high levels of superoxide.
The structure of the Caenorhabditis elegans manganese superoxide dismutase MnSOD-3-azide complex.,Hunter GJ, Trinh CH, Bonetta R, Stewart EE, Cabelli DE, Hunter T Protein Sci. 2015 Nov;24(11):1777-88. doi: 10.1002/pro.2768. Epub 2015 Aug 27. PMID:26257399[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hunter GJ, Trinh CH, Bonetta R, Stewart EE, Cabelli DE, Hunter T. The structure of the Caenorhabditis elegans manganese superoxide dismutase MnSOD-3-azide complex. Protein Sci. 2015 Nov;24(11):1777-88. doi: 10.1002/pro.2768. Epub 2015 Aug 27. PMID:26257399 doi:http://dx.doi.org/10.1002/pro.2768
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