2pex
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2pex' size='340' side='right'caption='[[2pex]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2pex' size='340' side='right'caption='[[2pex]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2pex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2pex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEX 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]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></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=2pex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pex OCA], [https://pdbe.org/2pex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pex RCSB], [https://www.ebi.ac.uk/pdbsum/2pex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pex 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=2pex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pex OCA], [https://pdbe.org/2pex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pex RCSB], [https://www.ebi.ac.uk/pdbsum/2pex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pex ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q93R11_XANCH Q93R11_XANCH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 20: | ||
</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=2pex 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=2pex ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The Xanthomonas campestris transcription regulator OhrR contains a reactive cysteine residue (C22) that upon oxidation by organic hydroperoxides (OHPs) forms an intersubunit disulphide bond with residue C127'. Such modification induces the expression of a peroxidase that reduces OHPs to their less toxic alcohols. Here, we describe the structures of reduced and OHP-oxidized OhrR, visualizing the structural mechanism of OHP induction. Reduced OhrR takes a canonical MarR family fold with C22 and C127' separated by 15.5 A. OHP oxidation results in the disruption of the Y36'-C22-Y47' interaction network and dissection of helix alpha5, which then allows the 135 degrees rotation and 8.2 A translation of C127', formation of the C22-C127' disulphide bond, and alpha6-alpha6' helix-swapped reconfiguration of the dimer interface. These changes result in the 28 degrees rigid body rotations of each winged helix-turn-helix motif and DNA dissociation. Similar effector-induced rigid body rotations are expected for most MarR family members. | ||
| - | |||
| - | Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR.,Newberry KJ, Fuangthong M, Panmanee W, Mongkolsuk S, Brennan RG Mol Cell. 2007 Nov 30;28(4):652-64. PMID:18042459<ref>PMID:18042459</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2pex" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]] | *[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bacillus campestris pammel 1895]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Xanthomonas campestris]] |
| - | [[Category: | + | [[Category: Brennan RG]] |
| - | [[Category: | + | [[Category: Newberry KJ]] |
Current revision
Structure of reduced C22S OhrR from Xanthamonas Campestris
| |||||||||||
