9ygl: Difference between revisions

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'''Unreleased structure'''


The entry 9ygl is ON HOLD  until Paper Publication
==RCK Gating Ring from Kch in the closed conformation==
<StructureSection load='9ygl' size='340' side='right'caption='[[9ygl]], [[Resolution|resolution]] 2.88&Aring;' 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]] 2.88&#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=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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]