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| | ==Crystal structure of Dps from Staphylococcus aureus== | | ==Crystal structure of Dps from Staphylococcus aureus== |
| - | <StructureSection load='2d5k' size='340' side='right' caption='[[2d5k]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='2d5k' size='340' side='right'caption='[[2d5k]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2d5k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staac Staac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D5K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2d5k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D5K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ji5|1ji5]], [[1jig|1jig]], [[1n1q|1n1q]], [[1qgh|1qgh]], [[1umn|1umn]], [[1dps|1dps]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=2d5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5k OCA], [https://pdbe.org/2d5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d5k RCSB], [https://www.ebi.ac.uk/pdbsum/2d5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d5k 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=2d5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5k OCA], [http://pdbe.org/2d5k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d5k RCSB], [http://www.ebi.ac.uk/pdbsum/2d5k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d5k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H2X069_STAAC A0A0H2X069_STAAC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2d5k" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2d5k" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Staac]] | + | [[Category: Staphylococcus aureus subsp. aureus COL]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Tanaka I]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Watanabe, N]] | + | [[Category: Watanabe N]] |
| - | [[Category: Yao, M]] | + | [[Category: Yao M]] |
| - | [[Category: Four helix bundle]]
| + | |
| - | [[Category: Metal binding protein]]
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| Structural highlights
Function
A0A0H2X069_STAAC
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Staphylococcus aureus MrgA (encoded by mrgA) belongs to the Dps family of proteins, which play important roles in coping with various stresses. The staphylococcal mrgA gene is specifically expressed under oxidative stress conditions and is one of the most highly induced genes during phagocytic killing by macrophages. We previously reported that mrgA is essential for oxidative stress resistance, and can cause nucleoid compaction. However, whether nucleoid compaction by itself would contribute to oxidative stress resistance was hard to determine, because Dps family proteins generally have ferroxidase activity to prevent hydroxyl radical formation via the Fenton reaction. In this study, we resolved the crystal structure of MrgA and conducted mutation analysis of Asp56 and Glu60, which are located at the expected ferroxidase centre. In the strain expressing Asp56Ala/Glu60Ala MrgA (termed MrgA*), MrgA* retained dodecamer formation and nucleoid compaction ability. By contrast, the ferroxidase activity of MrgA* decreased by about half. Viability of the mrgA* strain was as low as the mrgA null mutant in oxidative stress and phagocytic killing assays. These results suggest that nucleoid compaction by itself is insufficient for oxidative stress resistance, and Asp56 and Glu60 constitute essential molecular sites in MrgA for oxidative stress resistance and survival against phagocytic killing.
Nucleoid compaction by MrgA(Asp56Ala/Glu60Ala) does not contribute to staphylococcal cell survival against oxidative stress and phagocytic killing by macrophages.,Ushijima Y, Ohniwa RL, Maruyama A, Saito S, Tanaka Y, Morikawa K FEMS Microbiol Lett. 2014 Nov;360(2):144-51. doi: 10.1111/1574-6968.12598. Epub, 2014 Oct 21. PMID:25227518[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ushijima Y, Ohniwa RL, Maruyama A, Saito S, Tanaka Y, Morikawa K. Nucleoid compaction by MrgA(Asp56Ala/Glu60Ala) does not contribute to staphylococcal cell survival against oxidative stress and phagocytic killing by macrophages. FEMS Microbiol Lett. 2014 Nov;360(2):144-51. doi: 10.1111/1574-6968.12598. Epub, 2014 Oct 21. PMID:25227518 doi:http://dx.doi.org/10.1111/1574-6968.12598
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