6elk: Difference between revisions
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==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 10:27, 6 December 2017
C.elegans MnSOD-3 mutant - Q142HC.elegans MnSOD-3 mutant - Q142H
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 PubMedWe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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