View source for 9cb6


==Crystal Structure of RT-PhyR (ruthe_02744)==
<StructureSection load='9cb6' size='340' side='right'caption='[[9cb6]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cb6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rubellimicrobium_thermophilum_DSM_16684 Rubellimicrobium thermophilum DSM 16684]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CB6 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]] 2.83&#8491;</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=9cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cb6 OCA], [https://pdbe.org/9cb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cb6 RCSB], [https://www.ebi.ac.uk/pdbsum/9cb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cb6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S9QU65_9RHOB S9QU65_9RHOB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The general stress response (GSR) protects bacteria from a wide range of stressors. In Alphaproteobacteria, GSR activation is coordinated by HWE/HisKA2 family histidine kinases (HKs), which can exhibit noncanonical structure and function. For example, while most light-oxygen-voltage sensor-containing HKs are light-activated dimers, the Rubellimicrobium thermophilum RT-HK has inverted "dark on, light off" signaling logic with a tunable monomer/dimer equilibrium. Here, we further investigate these atypical behaviors of RT-HK and characterize its downstream signaling network. Using hydrogen-deuterium exchange mass spectrometry, we find that RT-HK uses a signal transduction mechanism similar to light-activated systems, despite its inverted logic. Mutagenesis reveals that RT-HK autophosphorylates in trans, with changes to the Jalpha helix linking sensor and kinase domains affecting autophosphorylation levels. Exploring downstream effects of RT-HK, we identified two GSR genetic regions, each encoding a copy of the central regulator PhyR. In vitro measurements of phosphotransfer from RT-HK to the two putative PhyRs revealed that RT-HK signals only to one and does so at an increased intensity in the dark, consistent with its reversed logic. X-ray crystal structures of both PhyRs revealed a substantial shift within the receiver domain of one, suggesting a basis for RT-HK specificity. We probed further down the pathway using nuclear magnetic resonance to determine that the single NepR homolog interacts with both unphosphorylated PhyRs, and this interaction is decoupled from activation in one PhyR. This work expands our understanding of HWE/HisKA2 family signal transduction, revealing marked variations from signaling mechanisms previously identified in other GSR networks.

,  PMID:40273983<ref>PMID:40273983</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cb6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rubellimicrobium thermophilum DSM 16684]]
[[Category: Gardner KH]]
[[Category: Isiorho EA]]
[[Category: Swingle D]]