View source for 7ux1


==EcMscK in an Open Conformation==
<StructureSection load='7ux1' size='340' side='right'caption='[[7ux1]], [[Resolution|resolution]] 3.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ux1]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UX1 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]] 3.48&#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=7ux1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ux1 OCA], [https://pdbe.org/7ux1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ux1 RCSB], [https://www.ebi.ac.uk/pdbsum/7ux1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ux1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSCK_ECOLI MSCK_ECOLI] Mechanosensitive channel that opens in response to membrane tension and specific ionic conditions. Requires high concentrations of external K(+), NH(4)(+), Rb(+) or Cs(+) to gate. May participate in the regulation of osmotic pressure changes within the cell, although it does not appear to have a major role in osmolarity regulation. Forms an ion channel of 1.0 nanosiemens conductance. The channel can remain active for between 30 seconds and over 3 minutes; it does not desensitize upon extended pressure. Its activity is masked in wild-type cells by the MscS channel.<ref>PMID:10202137</ref> <ref>PMID:11985727</ref> <ref>PMID:12374733</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mechanosensitive channels of small conductance, found in many living organisms, open under elevated membrane tension and thus play crucial roles in biological response to mechanical stress. Amongst these channels, MscK is unique in that its activation also requires external potassium ions. To better understand this dual gating mechanism by force and ligand, we elucidate distinct structures of MscK along the gating cycle using cryo-electron microscopy. The heptameric channel comprises three layers: a cytoplasmic domain, a periplasmic gating ring, and a markedly curved transmembrane domain that flattens and expands upon channel opening, which is accompanied by dilation of the periplasmic ring. Furthermore, our results support a potentially unifying mechanotransduction mechanism in ion channels depicted as flattening and expansion of the transmembrane domain.

Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel.,Mount J, Maksaev G, Summers BT, Fitzpatrick JAJ, Yuan P Nat Commun. 2022 Nov 12;13(1):6904. doi: 10.1038/s41467-022-34737-0. PMID:36371466<ref>PMID:36371466</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ux1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Mount JW]]
[[Category: Yuan P]]