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4a5m

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==Redox regulator HypR in its oxidized form==
==Redox regulator HypR in its oxidized form==
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<StructureSection load='4a5m' size='340' side='right' caption='[[4a5m]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4a5m' size='340' side='right'caption='[[4a5m]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4a5m]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A5M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4a5m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A5M FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
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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]] 3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a5n|4a5n]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a5m RCSB], [http://www.ebi.ac.uk/pdbsum/4a5m PDBsum]</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=4a5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5m OCA], [https://pdbe.org/4a5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a5m RCSB], [https://www.ebi.ac.uk/pdbsum/4a5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5m ProSAT]</span></td></tr>
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<table>
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</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/YYBR_BACSU YYBR_BACSU]
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Bacillus subtilis encodes redox-sensing MarR-type regulators of the OhrR and DUF24-families that sense organic hydroperoxides, diamide, quinones or aldehydes via thiol-based redox-switches. In this article, we characterize the novel redox-sensing MarR/DUF24-family regulator HypR (YybR) that is activated by disulphide stress caused by diamide and NaOCl in B. subtilis. HypR controls positively a flavin oxidoreductase HypO that confers protection against NaOCl stress. The conserved N-terminal Cys14 residue of HypR has a lower pK(a) of 6.36 and is essential for activation of hypO transcription by disulphide stress. HypR resembles a 2-Cys-type regulator that is activated by Cys14-Cys49' intersubunit disulphide formation. The crystal structures of reduced and oxidized HypR proteins were resolved revealing structural changes of HypR upon oxidation. In reduced HypR a hydrogen-bonding network stabilizes the reactive Cys14 thiolate that is 8-9 A apart from Cys49'. HypR oxidation breaks these H-bonds, reorients the monomers and moves the major groove recognition alpha4 and alpha4' helices approximately 4 A towards each other. This is the first crystal structure of a redox-sensing MarR/DUF24 family protein in bacteria that is activated by NaOCl stress. Since hypochloric acid is released by activated macrophages, related HypR-like regulators could function to protect pathogens against the host immune defense.
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Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.,Palm GJ, Khanh Chi B, Waack P, Gronau K, Becher D, Albrecht D, Hinrichs W, Read RJ, Antelmann H Nucleic Acids Res. 2012 May 1;40(9):4178-92. Epub 2012 Jan 11. PMID:22238377<ref>PMID:22238377</ref>
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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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Hinrichs, W.]]
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[[Category: Large Structures]]
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[[Category: Palm, G J.]]
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[[Category: Hinrichs W]]
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[[Category: Read, R J.]]
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[[Category: Palm GJ]]
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[[Category: Waack, P.]]
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[[Category: Read RJ]]
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[[Category: Activator]]
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[[Category: Waack P]]
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[[Category: Dna-binding]]
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[[Category: Transcription]]
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Current revision

Redox regulator HypR in its oxidized form

PDB ID 4a5m

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