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| | ==The structure of a reduced form of OxyR from N. meningitidis== | | ==The structure of a reduced form of OxyR from N. meningitidis== |
| - | <StructureSection load='3jv9' size='340' side='right' caption='[[3jv9]], [[Resolution|resolution]] 2.39Å' scene=''> | + | <StructureSection load='3jv9' size='340' side='right'caption='[[3jv9]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3jv9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JV9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3jv9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JV9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.39Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB0173 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</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=3jv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jv9 OCA], [https://pdbe.org/3jv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jv9 RCSB], [https://www.ebi.ac.uk/pdbsum/3jv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jv9 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=3jv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jv9 OCA], [http://pdbe.org/3jv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jv9 RCSB], [http://www.ebi.ac.uk/pdbsum/3jv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jv9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9K1H8_NEIMB Q9K1H8_NEIMB] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/3jv9_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/3jv9_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3jv9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3jv9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Neimb]] | + | [[Category: Large Structures]] |
| - | [[Category: OPPF, Oxford Protein Production Facility]] | + | [[Category: Neisseria meningitidis MC58]] |
| - | [[Category: Owens, R J]] | + | [[Category: Owens RJ]] |
| - | [[Category: Ren, J]] | + | [[Category: Ren J]] |
| - | [[Category: Sainsbury, S]] | + | [[Category: Sainsbury S]] |
| - | [[Category: Stuart, D I]] | + | [[Category: Stuart DI]] |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Lttr]]
| + | |
| - | [[Category: Lysr-type transcriptional regulator]]
| + | |
| - | [[Category: Oppf]]
| + | |
| - | [[Category: Oppf3291]]
| + | |
| - | [[Category: Oxford protein production facility]]
| + | |
| - | [[Category: Redox]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
Q9K1H8_NEIMB
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
BACKGROUND: Survival of the human pathogen, Neisseria meningitidis, requires an effective response to oxidative stress resulting from the release of hydrogen peroxide by cells of the human immune system. In N. meningitidis, expression of catalase, which is responsible for detoxifying hydrogen peroxide, is controlled by OxyR, a redox responsive LysR-type regulator. OxyR responds directly to intracellular hydrogen peroxide through the reversible formation of a disulphide bond between C199 and C208 in the regulatory domain of the protein. RESULTS: We report the first crystal structure of the regulatory domain of an OxyR protein (NMB0173 from N. meningitidis) in the reduced state i.e. with cysteines at positions 199 and 208. The protein was crystallized under reducing conditions and the structure determined to a resolution of 2.4 A. The overall fold of the Neisseria OxyR shows a high degree of similarity to the structure of a C199S mutant OxyR from E. coli, which cannot form the redox sensitive disulphide. In the neisserial structure, C199 is located at the start of helix alpha3, separated by 18 A from C208, which is positioned between helices alpha3 and alpha4. In common with other LysR-type regulators, full length OxyR proteins are known to assemble into tetramers. Modelling of the full length neisserial OxyR as a tetramer indicated that C199 and C208 are located close to the dimer-dimer interface in the assembled tetramer. The formation of the C199-C208 disulphide may thus affect the quaternary structure of the protein. CONCLUSION: Given the high level of structural similarity between OxyR from N. meningitidis and E. coli, we conclude that the redox response mechanism is likely to be similar in both species, involving the reversible formation of a disulphide between C199-C208. Modelling suggests that disulphide formation would directly affect the interface between regulatory domains in an OxyR tetramer which in turn may lead to an alteration in the spacing/orientation of the DNA-binding domains and hence the interaction of OxyR with its DNA binding sites.
The structure of a reduced form of OxyR from Neisseria meningitidis.,Sainsbury S, Ren J, Nettleship JE, Saunders NJ, Stuart DI, Owens RJ BMC Struct Biol. 2010 May 17;10:10. PMID:20478059[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sainsbury S, Ren J, Nettleship JE, Saunders NJ, Stuart DI, Owens RJ. The structure of a reduced form of OxyR from Neisseria meningitidis. BMC Struct Biol. 2010 May 17;10:10. PMID:20478059 doi:10.1186/1472-6807-10-10
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