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| | ==Crystal structure of OxyR from Porphyromonas gingivalis== | | ==Crystal structure of OxyR from Porphyromonas gingivalis== |
| - | <StructureSection load='3ho7' size='340' side='right' caption='[[3ho7]], [[Resolution|resolution]] 1.58Å' scene=''> | + | <StructureSection load='3ho7' size='340' side='right'caption='[[3ho7]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ho7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33277 Atcc 33277]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HO7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ho7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33277 Atcc 33277]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HO7 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oxyR, PG_0270 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=837 ATCC 33277])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oxyR, PG_0270 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=837 ATCC 33277])</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=3ho7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho7 OCA], [http://pdbe.org/3ho7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ho7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ho7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ho7 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=3ho7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho7 OCA], [https://pdbe.org/3ho7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ho7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ho7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ho7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| | ==See Also== | | ==See Also== |
| - | *[[Transcriptional activator|Transcriptional activator]] | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 33277]] | | [[Category: Atcc 33277]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Lewis, J P]] | | [[Category: Lewis, J P]] |
| | [[Category: Svintradze, D V]] | | [[Category: Svintradze, D V]] |
| Structural highlights
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
OxyR transcriptionally regulates Escherichia coli oxidative stress response genes through a reversibly reducible cysteine disulfide biosensor of cellular redox status. Structural changes induced by redox changes in these cysteines are conformationally transmitted to the dimer subunit interfaces, which alters dimer and tetramer interactions with DNA. In contrast to E. coli OxyR regulatory-domain structures, crystal structures of Porphyromonas gingivalis OxyR regulatory domains show minimal differences in dimer configuration on changes in cysteine disulfide redox status. This locked configuration of the P. gingivalis OxyR regulatory-domain dimer closely resembles the oxidized (activating) form of the E. coli OxyR regulatory-domain dimer. It correlates with the observed constitutive activation of some oxidative stress genes in P. gingivalis and is attributable to a single amino-acid insertion in P. gingivalis OxyR relative to E. coli OxyR. Modelling of full-length P. gingivalis, E. coli and Neisseria meningitidis OxyR-DNA complexes predicts different modes of DNA binding for the reduced and oxidized forms of each.
Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis.,Svintradze DV, Peterson DL, Collazo-Santiago EA, Lewis JP, Wright HT Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2091-103. doi:, 10.1107/S0907444913019471. Epub 2013 Sep 20. PMID:24100327[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Svintradze DV, Peterson DL, Collazo-Santiago EA, Lewis JP, Wright HT. Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis. Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2091-103. doi:, 10.1107/S0907444913019471. Epub 2013 Sep 20. PMID:24100327 doi:http://dx.doi.org/10.1107/S0907444913019471
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