5n57: Difference between revisions
New page: '''Unreleased structure''' The entry 5n57 is ON HOLD until Paper Publication Authors: Barwinska-Sendra, A., Basle, A., Waldron, K. Description: Staphylococcus aureus cambialistic super... |
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==Staphylococcus aureus cambialistic superoxide dismutase SodM== | |||
<StructureSection load='5n57' size='340' side='right'caption='[[5n57]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n57]] 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=5N57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N57 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=5n57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n57 OCA], [https://pdbe.org/5n57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n57 RCSB], [https://www.ebi.ac.uk/pdbsum/5n57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n57 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
The pathogenicity of Staphylococcus aureus is enhanced by having two superoxide dismutases (SODs): a Mn-specific SOD and another that can use either Mn or Fe. Using 94 GHz electron-nuclear double resonance (ENDOR) and electron double resonance detected (ELDOR)-NMR we show that, despite their different metal-specificities, their structural and electronic similarities extend down to their active-site (1)H- and (14)N-Mn(ii) hyperfine interactions. However these interactions, and hence the positions of these nuclei, are different in the inactive Mn-reconstituted Escherichia coli Fe-specific SOD. Density functional theory modelling attributes this to a different angular position of the E. coli H171 ligand. This likely disrupts the Mn-H171-E170' triad causing a shift in charge and in metal redox potential, leading to the loss of activity. This is supported by the correlated differences in the Mn(ii) zero-field interactions of the three SOD types and suggests that the triad is important for determining metal specific activity. | |||
A charge polarization model for the metal-specific activity of superoxide dismutases.,Barwinska-Sendra A, Basle A, Waldron KJ, Un S Phys Chem Chem Phys. 2018 Jan 24;20(4):2363-2372. doi: 10.1039/c7cp06829h. PMID:29308487<ref>PMID:29308487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5n57" style="background-color:#fffaf0;"></div> | ||
[[Category: Basle | |||
[[Category: | ==See Also== | ||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | |||
[[Category: Barwinska-Sendra A]] | |||
[[Category: Basle A]] | |||
[[Category: Waldron K]] | |||
Latest revision as of 21:02, 8 November 2023
Staphylococcus aureus cambialistic superoxide dismutase SodMStaphylococcus aureus cambialistic superoxide dismutase SodM
Structural highlights
FunctionSODM2_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).[1] [2] Publication Abstract from PubMedThe pathogenicity of Staphylococcus aureus is enhanced by having two superoxide dismutases (SODs): a Mn-specific SOD and another that can use either Mn or Fe. Using 94 GHz electron-nuclear double resonance (ENDOR) and electron double resonance detected (ELDOR)-NMR we show that, despite their different metal-specificities, their structural and electronic similarities extend down to their active-site (1)H- and (14)N-Mn(ii) hyperfine interactions. However these interactions, and hence the positions of these nuclei, are different in the inactive Mn-reconstituted Escherichia coli Fe-specific SOD. Density functional theory modelling attributes this to a different angular position of the E. coli H171 ligand. This likely disrupts the Mn-H171-E170' triad causing a shift in charge and in metal redox potential, leading to the loss of activity. This is supported by the correlated differences in the Mn(ii) zero-field interactions of the three SOD types and suggests that the triad is important for determining metal specific activity. A charge polarization model for the metal-specific activity of superoxide dismutases.,Barwinska-Sendra A, Basle A, Waldron KJ, Un S Phys Chem Chem Phys. 2018 Jan 24;20(4):2363-2372. doi: 10.1039/c7cp06829h. PMID:29308487[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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