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TitleStructure of the voltage-gated K⁺ channel Eag1 reveals an alternative voltage sensing mechanism.
Journal, issue, pagesScience, Vol. 353, Issue 6300, Page 664-669, Year 2016
Publish dateAug 12, 2016
AuthorsJonathan R Whicher / Roderick MacKinnon /
PubMed AbstractVoltage-gated potassium (K(v)) channels are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4-S5 linker, to the potassium pore. We determined the ...Voltage-gated potassium (K(v)) channels are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4-S5 linker, to the potassium pore. We determined the single-particle cryo-electron microscopy structure of mammalian K(v)10.1, or Eag1, bound to the channel inhibitor calmodulin, at 3.78 angstrom resolution. Unlike previous K(v) structures, the S4-S5 linker of Eag1 is a five-residue loop and the transmembrane segments are not domain swapped, which suggest an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4-S5 linker allow calmodulin to bind to the intracellular domains and to close the potassium pore, independent of voltage-sensor position. The structure reveals an alternative gating mechanism for K(v) channels and provides a template to further understand the gating properties of Eag1 and related channels.
External linksScience / PubMed:27516594 / PubMed Central
MethodsEM (single particle)
Resolution3.78 Å
Structure data

8215

5k7l

EMDB-8215, PDB-5k7l:
Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 bound to the channel inhibitor calmodulin
Method: EM (single particle) / Resolution: 3.78 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
KeywordsMETAL TRANSPORT/CALCIUM BINDING PROTEIN / Voltage-gated potassium channel / calmodulin / Cryoelectron microscopy / Eag1 / METAL TRANSPORT-CALCIUM BINDING PROTEIN complex

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