1z9c
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1z9c' size='340' side='right'caption='[[1z9c]], [[Resolution|resolution]] 2.64Å' scene=''> | <StructureSection load='1z9c' size='340' side='right'caption='[[1z9c]], [[Resolution|resolution]] 2.64Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1z9c]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1z9c]] is a 12 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=1Z9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z9C 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]] 2.64Å</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=1z9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9c OCA], [https://pdbe.org/1z9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z9c RCSB], [https://www.ebi.ac.uk/pdbsum/1z9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z9c 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=1z9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9c OCA], [https://pdbe.org/1z9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z9c RCSB], [https://www.ebi.ac.uk/pdbsum/1z9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z9c 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]] | ||
| Line 19: | Line 19: | ||
</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=1z9c 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=1z9c 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. | ||
| - | |||
| - | Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.,Hong M, Fuangthong M, Helmann JD, Brennan RG Mol Cell. 2005 Oct 7;20(1):131-41. PMID:16209951<ref>PMID:16209951</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1z9c" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 35: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Brennan | + | [[Category: Brennan RG]] |
| - | [[Category: Fuangthong | + | [[Category: Fuangthong M]] |
| - | [[Category: Helmann | + | [[Category: Helmann JD]] |
| - | [[Category: Hong | + | [[Category: Hong M]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of OhrR bound to the ohrA promoter: Structure of MarR family protein with operator DNA
| |||||||||||
