5n57: Difference between revisions
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<StructureSection load='5n57' size='340' side='right' caption='[[5n57]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='5n57' size='340' side='right' caption='[[5n57]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5n57]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N57 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5n57]] 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=5N57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N57 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sodA, sodM, A4U86_04870, BN1321_40056, ERS072738_00830, ERS072840_00559, ERS073147_02394, ERS073767_02269, ERS074020_00889, ERS1058648_00955, FORC27_0128, HMPREF3211_00238, SAMEA2298760_02426 ([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='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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5n57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n57 OCA], [http://pdbe.org/5n57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n57 RCSB], [http://www.ebi.ac.uk/pdbsum/5n57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n57 ProSAT]</span></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=5n57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n57 OCA], [http://pdbe.org/5n57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n57 RCSB], [http://www.ebi.ac.uk/pdbsum/5n57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n57 ProSAT]</span></td></tr> | ||
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== Function == | == 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] | [[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] | ||
<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> | |||
</div> | |||
<div class="pdbe-citations 5n57" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||