3n0r: Difference between revisions
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< | ==Structure of the PhyR stress response regulator at 1.25 Angstrom resolution== | ||
<StructureSection load='3n0r' size='340' side='right'caption='[[3n0r]], [[Resolution|resolution]] 1.25Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3n0r]] is a 1 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=3N0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N0R 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]] 1.251Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=3n0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n0r OCA], [https://pdbe.org/3n0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n0r RCSB], [https://www.ebi.ac.uk/pdbsum/3n0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n0r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9A2S9_CAUVC Q9A2S9_CAUVC] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n0/3n0r_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3n0r ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
PhyR is a hybrid stress regulator conserved in alpha-proteobacteria that contains an N-terminal sigma-like (SL) domain and a C-terminal receiver domain. Phosphorylation of the receiver domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. We present genetic evidence that Caulobacter crescentus PhyR is a phosphorylation-dependent stress regulator that functions in the same pathway as sigma(T) and its anti-sigma factor, NepR. Additionally, we report the X-ray crystal structure of PhyR at 1.25 A resolution, which provides insight into the mechanism of anti-anti-sigma regulation. Direct intramolecular contact between the PhyR receiver and SL domains spans regions sigma and sigma, likely serving to stabilize the SL domain in a closed conformation. The molecular surface of the receiver domain contacting the SL domain is the structural equivalent of alpha4-beta5-alpha5, which is known to undergo dynamic conformational change upon phosphorylation in a diverse range of receiver proteins. We propose a structural model of PhyR regulation in which receiver phosphorylation destabilizes the intramolecular interaction between SL and receiver domains, thereby permitting regions sigma and sigma in the SL domain to open about a flexible connector loop and bind anti-sigma factor. | |||
A structural model of anti-anti-sigma inhibition by a two-component receiver domain: the PhyR stress response regulator.,Herrou J, Foreman R, Fiebig A, Crosson S Mol Microbiol. 2010 Oct;78(2):290-304. doi:, 10.1111/j.1365-2958.2010.07323.x. Epub 2010 Aug 18. PMID:20735776<ref>PMID:20735776</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3n0r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Caulobacter vibrioides]] | [[Category: Caulobacter vibrioides]] | ||
[[Category: Crosson | [[Category: Large Structures]] | ||
[[Category: Herrou | [[Category: Crosson S]] | ||
[[Category: Herrou J]] | |||
Latest revision as of 05:09, 21 November 2024
Structure of the PhyR stress response regulator at 1.25 Angstrom resolutionStructure of the PhyR stress response regulator at 1.25 Angstrom resolution
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPhyR is a hybrid stress regulator conserved in alpha-proteobacteria that contains an N-terminal sigma-like (SL) domain and a C-terminal receiver domain. Phosphorylation of the receiver domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. We present genetic evidence that Caulobacter crescentus PhyR is a phosphorylation-dependent stress regulator that functions in the same pathway as sigma(T) and its anti-sigma factor, NepR. Additionally, we report the X-ray crystal structure of PhyR at 1.25 A resolution, which provides insight into the mechanism of anti-anti-sigma regulation. Direct intramolecular contact between the PhyR receiver and SL domains spans regions sigma and sigma, likely serving to stabilize the SL domain in a closed conformation. The molecular surface of the receiver domain contacting the SL domain is the structural equivalent of alpha4-beta5-alpha5, which is known to undergo dynamic conformational change upon phosphorylation in a diverse range of receiver proteins. We propose a structural model of PhyR regulation in which receiver phosphorylation destabilizes the intramolecular interaction between SL and receiver domains, thereby permitting regions sigma and sigma in the SL domain to open about a flexible connector loop and bind anti-sigma factor. A structural model of anti-anti-sigma inhibition by a two-component receiver domain: the PhyR stress response regulator.,Herrou J, Foreman R, Fiebig A, Crosson S Mol Microbiol. 2010 Oct;78(2):290-304. doi:, 10.1111/j.1365-2958.2010.07323.x. Epub 2010 Aug 18. PMID:20735776[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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