1z91
From Proteopedia
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==x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein== | ==x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein== | ||
| - | <StructureSection load='1z91' size='340' side='right' caption='[[1z91]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='1z91' size='340' side='right'caption='[[1z91]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1z91]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1z91]] is a 1 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=1Z91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z91 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z91 OCA], [https://pdbe.org/1z91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z91 RCSB], [https://www.ebi.ac.uk/pdbsum/1z91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z91 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/OHRR_BACSU OHRR_BACSU] Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements.<ref>PMID:11418552</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z91 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z91 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The mechanisms by which Bacillus subtilis OhrR, a member of the MarR family of transcription regulators, binds the ohrA operator and is induced by oxidation of its lone cysteine residue by organic hydroperoxides to sulphenic acid are unknown. Here, we describe the crystal structures of reduced OhrR and an OhrR-ohrA operator complex. To bind DNA, OhrR employs a chimeric winged helix-turn-helix DNA binding motif, which is composed of extended eukaryotic-like wings, prokaryotic helix-turn-helix motifs, and helix-helix elements. The reactivity of the peroxide-sensing cysteine is not modulated by proximal basic residues but largely by the positive dipole of helix alpha1. Induction originates from the alleviation of intersubunit steric clash between the sulphenic acid moieties of the oxidized sensor cysteines and nearby tyrosines and methionines. The structure of the OhrR-ohrA operator complex reveals the DNA binding mechanism of the entire MarR family and suggests a common inducer binding pocket. | ||
| - | + | ==See Also== | |
| - | + | *[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]] | |
| - | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Brennan RG]] |
| - | [[Category: | + | [[Category: Fuangthong M]] |
| - | + | [[Category: Helmann JD]] | |
| - | [[Category: | + | [[Category: Hong M]] |
| - | [[Category: | + | |
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Current revision
x-ray crystal structure of apo-OhrRC15S in reduced form: MarR family protein
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