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| | ==Crystal structure of a recombinant hybrid manganese superoxide dismutase from Staphylococcus equorum and Staphylococcus saprophyticus== | | ==Crystal structure of a recombinant hybrid manganese superoxide dismutase from Staphylococcus equorum and Staphylococcus saprophyticus== |
| - | <StructureSection load='5x2j' size='340' side='right' caption='[[5x2j]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='5x2j' size='340' side='right'caption='[[5x2j]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x2j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43958 Atcc 43958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X2J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X2J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x2j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_equorum Staphylococcus equorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X2J 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AST02_02815 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246432 ATCC 43958])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x2j OCA], [http://pdbe.org/5x2j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x2j RCSB], [http://www.ebi.ac.uk/pdbsum/5x2j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x2j ProSAT]</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=5x2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x2j OCA], [https://pdbe.org/5x2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x2j RCSB], [https://www.ebi.ac.uk/pdbsum/5x2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x2j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A1E5TT85_9STAP A0A1E5TT85_9STAP]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] | + | [https://www.uniprot.org/uniprot/A0A1E5TT85_9STAP A0A1E5TT85_9STAP] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] |
| | <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 5x2j" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5x2j" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43958]] | + | [[Category: Large Structures]] |
| - | [[Category: Arumsari, S]]
| + | |
| - | [[Category: Ismaya, W T]]
| + | |
| - | [[Category: Kamitori, S]]
| + | |
| - | [[Category: Retnoningrum, D S]]
| + | |
| - | [[Category: Yoshida, H]]
| + | |
| - | [[Category: Hybrid protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| | [[Category: Staphylococcus equorum]] | | [[Category: Staphylococcus equorum]] |
| - | [[Category: Staphylococcus saprophyticus]] | + | [[Category: Arumsari S]] |
| - | [[Category: Superoxide dismutase]] | + | [[Category: Ismaya WT]] |
| | + | [[Category: Kamitori S]] |
| | + | [[Category: Retnoningrum DS]] |
| | + | [[Category: Yoshida H]] |
| Structural highlights
Function
A0A1E5TT85_9STAP Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
Publication Abstract from PubMed
A recombinant Staphylococcus equorum manganese superoxide dismutase (MnSOD) with an Asp13Arg substitution displays activity over a wide range of pH, at high temperature and in the presence of chaotropic agents, and retains 50% of its activity after irradiation with UVC for up to 45 min. Interestingly, Bacillus subtilis MnSOD does not have the same stability, despite having a closely similar primary structure and thus presumably also tertiary structure. Here, the crystal structure of S. equorum MnSOD at 1.4 A resolution is reported that may explain these differences. The crystal belonged to space group P3221, with unit-cell parameters a = 57.36, b = 57.36, c = 105.76 A, and contained one molecule in the asymmetric unit. The symmetry operation indicates that the enzyme has a dimeric structure, as found in nature and in B. subtilis MnSOD. As expected, their overall structures are nearly identical. However, the loop connecting the helical and alpha/beta domains of S. equorum MnSOD is shorter than that in B. subtilis MnSOD, and adopts a conformation that allows more direct water-mediated hydrogen-bond interactions between the amino-acid side chains of the first and last alpha-helices in the latter domain. Furthermore, S. equorum MnSOD has a slightly larger buried area compared with the dimer surface area than that in B. subtilis MnSOD, while the residues that form the interaction in the dimer-interface region are highly conserved. Thus, the stability of S. equorum MnSOD may not originate from the dimeric form alone. Furthermore, an additional water molecule was found in the active site. This allows an alternative geometry for the coordination of the Mn atom in the active site of the apo form. This is the first structure of MnSOD from the genus Staphylococcus and may provide a template for the structural study of other MnSODs from this genus.
The first crystal structure of manganese superoxide dismutase from the genus Staphylococcus.,Retnoningrum DS, Yoshida H, Arumsari S, Kamitori S, Ismaya WT Acta Crystallogr F Struct Biol Commun. 2018 Mar 1;74(Pt 3):135-142. doi:, 10.1107/S2053230X18001036. Epub 2018 Feb 26. PMID:29497016[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Retnoningrum DS, Yoshida H, Arumsari S, Kamitori S, Ismaya WT. The first crystal structure of manganese superoxide dismutase from the genus Staphylococcus. Acta Crystallogr F Struct Biol Commun. 2018 Mar 1;74(Pt 3):135-142. doi:, 10.1107/S2053230X18001036. Epub 2018 Feb 26. PMID:29497016 doi:http://dx.doi.org/10.1107/S2053230X18001036
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