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| | <StructureSection load='4a5n' size='340' side='right'caption='[[4a5n]], [[Resolution|resolution]] 1.81Å' scene=''> | | <StructureSection load='4a5n' size='340' side='right'caption='[[4a5n]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a5n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A5N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a5n]] is a 4 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=4A5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A5N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.81Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a5m|4a5m]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=4a5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5n OCA], [http://pdbe.org/4a5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a5n RCSB], [http://www.ebi.ac.uk/pdbsum/4a5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5n 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=4a5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5n OCA], [https://pdbe.org/4a5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a5n RCSB], [https://www.ebi.ac.uk/pdbsum/4a5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a5n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/YYBR_BACSU YYBR_BACSU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Hinrichs, W]] | + | [[Category: Large Structures]] |
| - | [[Category: Palm, G J]] | + | [[Category: Hinrichs W]] |
| - | [[Category: Read, R J]] | + | [[Category: Palm GJ]] |
| - | [[Category: Waack, P]] | + | [[Category: Read RJ]] |
| - | [[Category: Activator]] | + | [[Category: Waack P]] |
| - | [[Category: Dna binding]]
| + | |
| - | [[Category: Marr-like]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
YYBR_BACSU
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Palm GJ, Khanh Chi B, Waack P, Gronau K, Becher D, Albrecht D, Hinrichs W, Read RJ, Antelmann H. Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR. Nucleic Acids Res. 2012 May 1;40(9):4178-92. Epub 2012 Jan 11. PMID:22238377 doi:10.1093/nar/gkr1316
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