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TitleMechanism of Kch activation by Zn.
Journal, issue, pagesPNAS Nexus, Vol. 5, Issue 9, Page pgag284, Year 2026
Publish dateAug 31, 2026
AuthorsBrian Morote-Costas / Yaping Pan / Lie Wang / Xiaochen Bai / Steve W Lockless / Ming Zhou /
PubMed Abstract has a single K channel gene, , 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 ... has a single K channel gene, , 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 or Cu 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 promotes the open conformation by stabilizing the assembly interface. These results expand our knowledge on Kch and on RCK-mediated regulation of ion channels.
External linksPNAS Nexus / PubMed:42729885 / PubMed Central
MethodsEM (single particle)
Resolution2.88 - 3.19 Å
Structure data

72842

9ye0

EMDB-72842, PDB-9ye0:
RCK Gating Ring from Kch in the open conformation
Method: EM (single particle) / Resolution: 2.88 Å

72908

9yfv

EMDB-72908, PDB-9yfv:
RCK Gating Ring from Kch in the Intermediate conformation
Method: EM (single particle) / Resolution: 2.92 Å

72932

9ygl

EMDB-72932, PDB-9ygl:
RCK Gating Ring from Kch in the closed conformation
Method: EM (single particle) / Resolution: 2.88 Å

73056

9ykq

EMDB-73056, PDB-9ykq:
RCK Gating Ring from Kch in the open conformation in the presence of zinc
Method: EM (single particle) / Resolution: 3.19 Å

Source
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / Ion Channel Gating ring / RCK / Potassium Channel / MEMBRANE PROTEIN

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