5n56: Difference between revisions
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New page: '''Unreleased structure''' The entry 5n56 is ON HOLD until Paper Publication Authors: Barwinska-Sendra, A., Basle, A., Waldron, K. Description: Staphylococcus aureus Mn-dependent super... |
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==Staphylococcus aureus Mn-dependent superoxide dismutase SodA== | |||
<StructureSection load='5n56' size='340' side='right'caption='[[5n56]], [[Resolution|resolution]] 2.07Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_RF122 Staphylococcus aureus RF122]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N56 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]] 2.07Å</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=5n56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n56 OCA], [https://pdbe.org/5n56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n56 RCSB], [https://www.ebi.ac.uk/pdbsum/5n56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n56 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SODM1_STAAB SODM1_STAAB] 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 == | |||
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 5n56" 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 RF122]] | |||
[[Category: Barwinska-Sendra A]] | |||
[[Category: Basle A]] | |||
[[Category: Waldron K]] | |||
