View source for 5frx


==crystal structure of the phenol-responsive sensory domain of the transcription activator PoxR in complex with 4-nitrophenol==
<StructureSection load='5frx' size='340' side='right'caption='[[5frx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5frx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ralstonia_sp._E2 Ralstonia sp. E2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FRX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5frx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frx OCA], [https://pdbe.org/5frx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5frx RCSB], [https://www.ebi.ac.uk/pdbsum/5frx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5frx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O84957_9RALS O84957_9RALS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Positive phenol-degradative gene regulator (PoxR) is a sigma(54)-dependent AAA+ ATPase transcription activator that regulates the catabolism of phenols. The PoxR sensory domain detects phenols and relays signals for the activation of transcription. Here we report the first structure of the phenol sensory domain bound to phenol and five derivatives. It exists as a tightly intertwined homodimer with a phenol-binding pocket buried inside, placing two C termini on the same side of the dimer. His102 and Trp130 interact with the hydroxyl group of the phenol in a cavity surrounded by rigid hydrophobic residues on one side and a flexible region on the other. Each monomer has a V4R fold with a unique zinc-binding site. A shift at the C-terminal helix suggests that there is a possible conformational change upon ligand binding. The results provide a structural basis of chemical effector binding for transcriptional regulation with broad implications for protein engineering.

Structural Analysis of the Phenol-Responsive Sensory Domain of the Transcription Activator PoxR.,Patil VV, Park KH, Lee SG, Woo E Structure. 2016 Apr 5;24(4):624-30. doi: 10.1016/j.str.2016.03.006. PMID:27050690<ref>PMID:27050690</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5frx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ralstonia sp. E2]]
[[Category: Patil VV]]
[[Category: Woo EJ]]