9ygl: Difference between revisions
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==RCK Gating Ring from Kch in the closed conformation== | |||
<StructureSection load='9ygl' size='340' side='right'caption='[[9ygl]], [[Resolution|resolution]] 2.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9ygl]] is a 8 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=9YGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YGL 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]] 2.88Å</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=9ygl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ygl OCA], [https://pdbe.org/9ygl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ygl RCSB], [https://www.ebi.ac.uk/pdbsum/9ygl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ygl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KCH_ECOLI KCH_ECOLI] K(+)-specific ion channel. May play a role in the defense against osmotic shock.<ref>PMID:8170937</ref> <ref>PMID:12912904</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Escherichia coli has a single K(+) channel gene, kch, that produces a K(+) channel with six transmembrane segments and a cytosolic Regulate Conductance of K(+) channels (RCK) domain. RCK domains are present in both eukaryotic and prokaryotic organisms and known to regulate ion channel activity upon binding of an ion or a nucleotide, however, how Kch is regulated remains unknown. Here, we show that Zn(2+) or Cu(2+) activates Kch via the RCK domain. Structural studies reveal that eight RCK domains assemble into a gating ring that can assume three conformations, closed, intermediate, and open, and that Zn(2+) promotes the open conformation by stabilizing the assembly interface. These results expand our knowledge on Kch and on RCK-mediated regulation of ion channels. | |||
Mechanism of Kch activation by Zn(2).,Morote-Costas B, Pan Y, Wang L, Bai X, Lockless SW, Zhou M PNAS Nexus. 2026 Aug 31;5(9):pgag284. doi: 10.1093/pnasnexus/pgag284. eCollection , 2026 Sep. PMID:42729885<ref>PMID:42729885</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9ygl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Morote-Costas B]] | |||
[[Category: Zhou M]] | |||
Latest revision as of 09:49, 30 September 2026
RCK Gating Ring from Kch in the closed conformation
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