3t0y: Difference between revisions
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[[ | ==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]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3t0y]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0Y FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC_3477, PhyR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides]), CC_3476, NepR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t0y RCSB], [http://www.ebi.ac.uk/pdbsum/3t0y PDBsum]</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Response regulator|Response regulator]] | *[[Response regulator|Response regulator]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Caulobacter vibrioides]] | [[Category: Caulobacter vibrioides]] | ||
[[Category: Crosson, S | [[Category: Crosson, S]] | ||
[[Category: Herrou, J | [[Category: Herrou, J]] | ||
[[Category: Anti-sigma factor]] | [[Category: Anti-sigma factor]] | ||
[[Category: Gene regulation]] | [[Category: Gene regulation]] | ||