9yfv | pdb_00009yfv

RCK Gating Ring from Kch in the Intermediate conformation

spinqualitylabelsall models 9yfv, resolution 2.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9yfv is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.92Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KCH_ECOLI K(+)-specific ion channel. May play a role in the defense against osmotic shock. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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