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| | <StructureSection load='3dc5' size='340' side='right'caption='[[3dc5]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3dc5' size='340' side='right'caption='[[3dc5]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dc5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DC5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dc5]] 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=3DC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DC5 FirstGlance]. <br> |
| - | </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></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"><div style='overflow: auto; max-height: 3em;'>[[3dc6|3dc6]]</div></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sod-3, C08A9.1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://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=3dc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dc5 OCA], [https://pdbe.org/3dc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dc5 RCSB], [https://www.ebi.ac.uk/pdbsum/3dc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dc5 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=3dc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dc5 OCA], [https://pdbe.org/3dc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dc5 RCSB], [https://www.ebi.ac.uk/pdbsum/3dc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dc5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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. |
| | == 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: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Superoxide dismutase]]
| + | [[Category: Hunter GJ]] |
| - | [[Category: Hunter, G J]] | + | [[Category: Hunter T]] |
| - | [[Category: Hunter, T]] | + | [[Category: Phillips SEV]] |
| - | [[Category: Phillips, S E.V]] | + | [[Category: Stewart EE]] |
| - | [[Category: Stewart, E E]] | + | [[Category: Trinh CH]] |
| - | [[Category: Trinh, C H]] | + | |
| - | [[Category: Alpha hairpin n domain]]
| + | |
| - | [[Category: Alpha/beta c domain]]
| + | |
| - | [[Category: Manganese]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Transit peptide]]
| + | |
| Structural highlights
Function
SODM2_CAEEL Destroys superoxide anion 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
Caenorhabditis elegans expresses two manganese superoxide dismutase enzymes (MnSOD-2 and MnSOD-3) that are targeted to the mitochondrion. MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible. The structures of these two mononuclear metalloenzymes have been determined to 1.8 and 1.7 A resolution, respectively. Pink crystals formed in space group P4(1)2(1)2 for each, with unit-cell parameters a = b = 81.0, c = 137.4 A for MnSOD-2 and a = b = 81.8, c = 136.0 A for MnSOD-3. The final structure of MnSOD-3 was refined to R = 21.6% and R(free) = 26.2% at 293 K, and R = 18.9% and R(free) = 22.6% at 100 K, while that of MnSOD-2 was refined to R = 16.9% and R(free) = 20.1% at 100 K. The asymmetric unit cell is comprised of two subunits. The resulting structures are very similar to that of human MnSOD and form a tetramer corresponding to a dimer of dimers. The subunit interface between dimers is comprised of two four-helix bundles that stabilize the biologically significant homotetramer.
Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans.,Trinh CH, Hunter T, Stewart EE, Phillips SE, Hunter GJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt, 12):1110-4. Epub 2008 Nov 28. PMID:19052361[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Trinh CH, Hunter T, Stewart EE, Phillips SE, Hunter GJ. Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 1;64(Pt, 12):1110-4. Epub 2008 Nov 28. PMID:19052361 doi:10.1107/S1744309108037056
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