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4x6g

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==Full-length OxyR C199D from pseudomonas aeruginosa==
==Full-length OxyR C199D from pseudomonas aeruginosa==
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<StructureSection load='4x6g' size='340' side='right' caption='[[4x6g]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4x6g' size='340' side='right'caption='[[4x6g]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4x6g]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X6G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4x6g]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X6G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xws|4xws]], [[4y0m|4y0m]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene></td></tr>
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<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=4x6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6g OCA], [http://pdbe.org/4x6g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x6g RCSB], [http://www.ebi.ac.uk/pdbsum/4x6g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6g ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6g OCA], [https://pdbe.org/4x6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x6g RCSB], [https://www.ebi.ac.uk/pdbsum/4x6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6g ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9HTL4_PSEAE Q9HTL4_PSEAE]
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OxyR, a bacterial peroxide sensor, is a LysR-type transcriptional regulator (LTTR) that regulates the transcription of defense genes in response to a low level of cellular H2O2. Consisting of an N-terminal DNA-binding domain (DBD) and a C-terminal regulatory domain (RD), OxyR senses H2O2 with conserved cysteine residues in the RD. However, the precise mechanism of OxyR is not yet known due to the absence of the full-length (FL) protein structure. Here we determined the crystal structures of the FL protein and RD of Pseudomonas aeruginosa OxyR and its C199D mutant proteins. The FL crystal structures revealed that OxyR has a tetrameric arrangement assembled via two distinct dimerization interfaces. The C199D mutant structures suggested that new interactions that are mediated by cysteine hydroxylation induce a large conformational change, facilitating intramolecular disulfide-bond formation. More importantly, a bound H2O2 molecule was found near the Cys199 site, suggesting the H2O2-driven oxidation mechanism of OxyR. Combined with the crystal structures, a modeling study suggested that a large movement of the DBD is triggered by structural changes in the regulatory domains upon oxidation. Taken together, these findings provide novel concepts for answering key questions regarding OxyR in the H2O2-sensing and oxidation-dependent regulation of antioxidant genes.
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Structural details of the OxyR peroxide-sensing mechanism.,Jo I, Chung IY, Bae HW, Kim JS, Song S, Cho YH, Ha NC Proc Natl Acad Sci U S A. 2015 May 19;112(20):6443-8. doi:, 10.1073/pnas.1424495112. Epub 2015 Apr 30. PMID:25931525<ref>PMID:25931525</ref>
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==See Also==
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4x6g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ha, N C]]
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[[Category: Large Structures]]
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[[Category: Jo, I]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Dna binding protein]]
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[[Category: Ha NC]]
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[[Category: Lysr]]
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[[Category: Jo I]]
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[[Category: Oxyr]]
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[[Category: Peroxide]]
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[[Category: Transcription regulator]]
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Current revision

Full-length OxyR C199D from pseudomonas aeruginosa

PDB ID 4x6g

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