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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 [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6QV9 FirstGlance]. <br> | + | <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='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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sodA, sodA_1, BN1321_260190, BTN44_04405, CSC83_01345, CSC87_02560, CV021_16580, EP54_01115, EQ90_12445, ERS072840_00871, HMPREF3211_01704, M1K003_1305, NCTC10654_01617, NCTC11940_01488, NCTC13131_01937, NCTC13196_02481, RK64_08340, SAMEA1466939_00978, SAMEA1708674_02019 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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='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'>[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'>[http://proteopedia.org/fgij/fg.htm?mol=6qv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv9 OCA], [http://pdbe.org/6qv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qv9 RCSB], [http://www.ebi.ac.uk/pdbsum/6qv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/W8TT57_STAAU W8TT57_STAAU]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] | + | [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: Superoxide dismutase]] | |
| - | [[Category: Barwinska-Sendra, A]] | |
| - | [[Category: Basle, A]] | |
| - | [[Category: Waldron, K]] | |
| - | [[Category: Cambialistic]] | |
| - | [[Category: Metalloenzyme]] | |
| - | [[Category: Oxidoreductase]] | |
| | [[Category: Staphylococcus aureus]] | | [[Category: Staphylococcus aureus]] |
| | + | [[Category: Barwinska-Sendra A]] |
| | + | [[Category: Basle A]] |
| | + | [[Category: Waldron K]] |
| Structural highlights
Function
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.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Clements MO, Watson SP, Foster SJ. Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol. 1999 Jul;181(13):3898-903. PMID:10383955 doi:10.1128/JB.181.13.3898-3903.1999
- ↑ Karavolos MH, Horsburgh MJ, Ingham E, Foster SJ. Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology (Reading). 2003 Oct;149(Pt 10):2749-2758. PMID:14523108 doi:10.1099/mic.0.26353-0
- ↑ Maalej S, Dammak I, Dukan S. The impairment of superoxide dismutase coordinates the derepression of the PerR regulon in the response of Staphylococcus aureus to HOCl stress. Microbiology (Reading). 2006 Mar;152(Pt 3):855-861. PMID:16514164 doi:10.1099/mic.0.28385-0
- ↑ 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. An evolutionary path to altered cofactor specificity in a metalloenzyme. Nat Commun. 2020 Jun 1;11(1):2738. doi: 10.1038/s41467-020-16478-0. PMID:32483131 doi:http://dx.doi.org/10.1038/s41467-020-16478-0
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