View source for 3t0y


==Structure of the PhyR anti-anti-sigma domain bound to the anti-sigma factor, NepR==
<StructureSection load='3t0y' size='340' side='right'caption='[[3t0y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3t0y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0Y 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]] 2.102&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3t0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0y OCA], [https://pdbe.org/3t0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0y RCSB], [https://www.ebi.ac.uk/pdbsum/3t0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0y ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Proteobacteria uniquely integrate features of two-component signal transduction (TCS) and alternative sigma factor (sigma) regulation to control transcription in response to general stress. The core of this regulatory system is the PhyR protein, which contains a sigma-like (SL) domain and a TCS receiver domain. Aspartyl phosphorylation of the PhyR receiver in response to stress signals promotes binding of the anti-sigma factor, NepR, to PhyR-SL. This mechanism, whereby NepR switches binding between its cognate sigma factor and phospho-PhyR (PhyR approximately P), controls transcription of the general stress regulon. We have defined the structural basis of the PhyR approximately P/NepR interaction in Caulobacter crescentus and characterized the effect of aspartyl phosphorylation on PhyR structure by molecular dynamics simulations. Our data support a model in which phosphorylation of the PhyR receiver domain promotes its dissociation from the PhyR-SL domain, which exposes the NepR binding site. A highly dynamic loop-helix region (alpha3-alpha4) of the PhyR-SL domain plays an important role in PhyR approximately P binding to NepR in vitro, and in stress-dependent activation of transcription in vivo. This study provides a foundation for understanding the protein-protein interactions and protein structural dynamics that underpin general stress adaptation in a large and metabolically diverse clade of the bacterial kingdom.

Structural basis of a protein partner switch that regulates the general stress response of alpha-proteobacteria.,Herrou J, Rotskoff G, Luo Y, Roux B, Crosson S Proc Natl Acad Sci U S A. 2012 May 22;109(21):E1415-23. Epub 2012 May 1. PMID:22550172<ref>PMID:22550172</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3t0y" style="background-color:#fffaf0;"></div>

==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caulobacter vibrioides]]
[[Category: Large Structures]]
[[Category: Crosson S]]
[[Category: Herrou J]]