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TitleCryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 114, Issue 17, Page 4430-4435, Year 2017
Publish dateApr 25, 2017
AuthorsZachary M James / Andrew J Borst / Yoni Haitin / Brandon Frenz / Frank DiMaio / William N Zagotta / David Veesler /
PubMed AbstractCyclic nucleotide-gated (CNG) and hyperpolarization-activated cyclic nucleotide-regulated (HCN) ion channels play crucial physiological roles in phototransduction, olfaction, and cardiac pace making. ...Cyclic nucleotide-gated (CNG) and hyperpolarization-activated cyclic nucleotide-regulated (HCN) ion channels play crucial physiological roles in phototransduction, olfaction, and cardiac pace making. These channels are characterized by the presence of a carboxyl-terminal cyclic nucleotide-binding domain (CNBD) that connects to the channel pore via a C-linker domain. Although cyclic nucleotide binding has been shown to promote CNG and HCN channel opening, the precise mechanism underlying gating remains poorly understood. Here we used cryoEM to determine the structure of the intact LliK CNG channel isolated from -which shares sequence similarity to eukaryotic CNG and HCN channels-in the presence of a saturating concentration of cAMP. A short S4-S5 linker connects nearby voltage-sensing and pore domains to produce a non-domain-swapped transmembrane architecture, which appears to be a hallmark of this channel family. We also observe major conformational changes of the LliK C-linkers and CNBDs relative to the crystal structures of isolated C-linker/CNBD fragments and the cryoEM structures of related CNG, HCN, and KCNH channels. The conformation of our LliK structure may represent a functional state of this channel family not captured in previous studies.
External linksProc Natl Acad Sci U S A / PubMed:28396445 / PubMed Central
MethodsEM (single particle)
Resolution4.2 Å
Structure data

8632

5v4s

EMDB-8632, PDB-5v4s:
CryoEM Structure of a Prokaryotic Cyclic Nucleotide-Gated Ion Channel
Method: EM (single particle) / Resolution: 4.2 Å

8633

5v4s

EMDB-8633, PDB-5v4s:
CryoEM Structure of a Prokaryotic Cyclic Nucleotide-Gated Ion Channel
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • leptospira licerasiae serovar varillal str. var 010 (bacteria)
KeywordsTRANSPORT PROTEIN / Ion channel / cyclic nucleotide / allostery / vision / olfaction

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