6qv9: Difference between revisions
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<StructureSection load='6qv9' size='340' side='right'caption='[[6qv9]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6qv9' size='340' side='right'caption='[[6qv9]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6qv9]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6qv9]] 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=6QV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QV9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <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'>[https://proteopedia.org/fgij/fg.htm?mol=6qv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv9 OCA], [https://pdbe.org/6qv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qv9 RCSB], [https://www.ebi.ac.uk/pdbsum/6qv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv9 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SODM1_STAA8 SODM1_STAA8] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in maintaining cell viability throughout all stages of growth, but may be the major SOD activity in the exponential growth-phase. 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 when the level of SOD activity is low.<ref>PMID:10383955</ref> <ref>PMID:14523108</ref> <ref>PMID:16514164</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6qv9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6qv9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Barwinska-Sendra A]] | |||
[[Category: Basle A]] | |||
[[Category: Waldron K]] | |||
Latest revision as of 15:09, 24 January 2024
Staphylococcus aureus superoxide dismutase SodA double mutantStaphylococcus aureus superoxide dismutase SodA double mutant
Structural highlights
FunctionSODM1_STAA8 Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in maintaining cell viability throughout all stages of growth, but may be the major SOD activity in the exponential growth-phase. 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 when the level of SOD activity is low.[1] [2] [3] Publication Abstract from PubMedAlmost 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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