5n56
From Proteopedia
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<StructureSection load='5n56' size='340' side='right' caption='[[5n56]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='5n56' size='340' side='right' caption='[[5n56]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5n56]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N56 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5n56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staab Staab]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N56 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, SAB1425c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273036 STAAB])</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=5n56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n56 OCA], [http://pdbe.org/5n56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n56 RCSB], [http://www.ebi.ac.uk/pdbsum/5n56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n56 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=5n56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n56 OCA], [http://pdbe.org/5n56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n56 RCSB], [http://www.ebi.ac.uk/pdbsum/5n56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n56 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://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. | [[http://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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5n56" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Staab]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
[[Category: Barwinska-Sendra, A]] | [[Category: Barwinska-Sendra, A]] | ||
Revision as of 07:53, 21 March 2018
Staphylococcus aureus Mn-dependent superoxide dismutase SodA
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