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6elk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==C.elegans MnSOD-3 mutant - Q142H== | |
| + | <StructureSection load='6elk' size='340' side='right' caption='[[6elk]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6elk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ELK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dc5|3dc5]], [[4x9q|4x9q]]</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=6elk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elk OCA], [http://pdbe.org/6elk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6elk RCSB], [http://www.ebi.ac.uk/pdbsum/6elk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6elk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have generated a site-directed mutant of the manganese superoxide dismutase SOD-3 of C.elegans (MnSOD-3) which modifies the metal specificity of the enzyme. While wild-type MnSOD-3 functions with manganese in the active site (3600 U.mg protein-1) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50% of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron. | ||
| - | + | A single mutation is sufficient to modify the metal selectivity and specificity of a eukaryotic manganese superoxide dismutase to encompass iron.,Hunter GJ, Hunter T, Trinh C, Bonetta R, Sacco A, Vella M, Sultana PM, Borowski T, Garcia-Fandino R, Stockner T, Fadia H Chemistry. 2017 Nov 26. doi: 10.1002/chem.201704655. PMID:29178484<ref>PMID:29178484</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Hunter, G | + | <div class="pdbe-citations 6elk" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Superoxide dismutase]] | ||
| + | [[Category: Hunter, G J]] | ||
[[Category: Hunter, T]] | [[Category: Hunter, T]] | ||
| + | [[Category: Trinh, C H]] | ||
| + | [[Category: Manganese]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 07:27, 6 December 2017
C.elegans MnSOD-3 mutant - Q142H
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