10rx: Difference between revisions
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==SthK closed state at low temperature, cAMP-bound in DOPC nanodiscs== | |||
<StructureSection load='10rx' size='340' side='right'caption='[[10rx]], [[Resolution|resolution]] 2.51Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[10rx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Spirochaeta_thermophila Spirochaeta thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=10RX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=10RX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.51Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</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=10rx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=10rx OCA], [https://pdbe.org/10rx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=10rx RCSB], [https://www.ebi.ac.uk/pdbsum/10rx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=10rx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G0GA88_WINT7 G0GA88_WINT7] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Temperature sensing enables organisms to detect and respond to environmental changes. While temperature-responsive ion channels are key to this process, the physico-chemical mechanisms by which they sense temperature remain poorly understood. Here, we investigate the molecular details of temperature sensing in the model bacterial channel, SthK from Spirochaeta thermophila. We show that SthK is cold sensitive, displaying higher activity below 30 degrees C. Remarkably, SthK cold sensitivity depends strongly on membrane lipids, being sensitive in amine-containing lipids but insensitive in anionic lipids. Combining cryo-EM structural analysis, mutagenesis, and functional assays, we identify an intersubunit salt bridge that acts as temperature sensor. This salt bridge forms only in closed states, and determines channel opening by controlling closed-state stability. Lower temperatures weaken salt-bridge interactions, favoring channel opening, and lipid headgroups tune temperature sensitivity by modulating salt-bridge strength. These findings highlight how thermosensitivity can emerge from cooperative interactions between protein and the surrounding membrane. | |||
Mechanism of lipid-dependent cold sensitivity in a model ion channel.,Li CC, Nimigean CM Nat Commun. 2026 Apr 10. doi: 10.1038/s41467-026-71714-3. PMID:41963351<ref>PMID:41963351</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 10rx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Spirochaeta thermophila]] | |||
[[Category: Chieh-Chin L]] | |||
[[Category: Nimigean CM]] | |||
Latest revision as of 08:01, 29 April 2026
SthK closed state at low temperature, cAMP-bound in DOPC nanodiscs
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