6qv8: Difference between revisions

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 <StructureSection load='6qv8' size='340' side='right'caption='[[6qv8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6qv8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QV8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6qv8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QV8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.5&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=6qv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv8 OCA], [http://pdbe.org/6qv8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qv8 RCSB], [http://www.ebi.ac.uk/pdbsum/6qv8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv8 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=6qv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv8 OCA], [https://pdbe.org/6qv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qv8 RCSB], [https://www.ebi.ac.uk/pdbsum/6qv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/W8UU58_STAAU W8UU58_STAAU]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
+[https://www.uniprot.org/uniprot/SODM2_STAA8 SODM2_STAA8] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal ion at the active site. May play a role in maintaining cell viability during the late-exponential and stationary phases of growth since it becomes a major source of activity under oxidative stress. Has a role in resisting external superoxide stress. Involved in acid tolerance and the acid-adaptive response. Mediates the derepression of perR regulon in the response to HOCl stress at low level of SOD activity (By similarity).<ref>PMID:11344148</ref> <ref>PMID:14523108</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Almost half of all enzymes utilize a metal cofactor. However, the features that dictate the metal utilized by metalloenzymes are poorly understood, limiting our ability to manipulate these enzymes for industrial and health-associated applications. The ubiquitous iron/manganese superoxide dismutase (SOD) family exemplifies this deficit, as the specific metal used by any family member cannot be predicted. Biochemical, structural and paramagnetic analysis of two evolutionarily related SODs with different metal specificity produced by the pathogenic bacterium Staphylococcus aureus identifies two positions that control metal specificity. These residues make no direct contacts with the metal-coordinating ligands but control the metal's redox properties, demonstrating that subtle architectural changes can dramatically alter metal utilization. Introducing these mutations into S. aureus alters the ability of the bacterium to resist superoxide stress when metal starved by the host, revealing that small changes in metal-dependent activity can drive the evolution of metalloenzymes with new cofactor specificity.
+An evolutionary path to altered cofactor specificity in a metalloenzyme.,Barwinska-Sendra A, Garcia YM, Sendra KM, Basle A, Mackenzie ES, Tarrant E, Card P, Tabares LC, Bicep C, Un S, Kehl-Fie TE, Waldron KJ Nat Commun. 2020 Jun 1;11(1):2738. doi: 10.1038/s41467-020-16478-0. PMID:32483131<ref>PMID:32483131</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6qv8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Superoxide dismutase]]
-[[Category: Barwinska-Sendra, A]]
-[[Category: Basle, A]]
-[[Category: Waldron, K]]
-[[Category: Cambialistic]]
-[[Category: Metalloenzyme]]
-[[Category: Oxidoreductase]]
 [[Category: Staphylococcus aureus]]
+[[Category: Barwinska-Sendra A]]
+[[Category: Basle A]]
+[[Category: Waldron K]]