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Structure paper

TitleElectromechanical coupling in the hyperpolarization-activated K channel KAT1.
Journal, issue, pagesNature, Vol. 583, Issue 7814, Page 145-149, Year 2020
Publish dateMay 27, 2020
AuthorsMichael David Clark / Gustavo F Contreras / Rong Shen / Eduardo Perozo /
PubMed AbstractVoltage-gated potassium (K) channels coordinate electrical signalling and control cell volume by gating in response to membrane depolarization or hyperpolarization. However, although voltage-sensing ...Voltage-gated potassium (K) channels coordinate electrical signalling and control cell volume by gating in response to membrane depolarization or hyperpolarization. However, although voltage-sensing domains transduce transmembrane electric field changes by a common mechanism involving the outward or inward translocation of gating charges, the general determinants of channel gating polarity remain poorly understood. Here we suggest a molecular mechanism for electromechanical coupling and gating polarity in non-domain-swapped K channels on the basis of the cryo-electron microscopy structure of KAT1, the hyperpolarization-activated K channel from Arabidopsis thaliana. KAT1 displays a depolarized voltage sensor, which interacts with a closed pore domain directly via two interfaces and indirectly via an intercalated phospholipid. Functional evaluation of KAT1 structure-guided mutants at the sensor-pore interfaces suggests a mechanism in which direct interaction between the sensor and the C-linker hairpin in the adjacent pore subunit is the primary determinant of gating polarity. We suggest that an inward motion of the S4 sensor helix of approximately 5-7 Å can underlie a direct-coupling mechanism, driving a conformational reorientation of the C-linker and ultimately opening the activation gate formed by the S6 intracellular bundle. This direct-coupling mechanism contrasts with allosteric mechanisms proposed for hyperpolarization-activated cyclic nucleotide-gated channels, and may represent an unexpected link between depolarization- and hyperpolarization-activated channels.
External linksNature / PubMed:32461693 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 3.8 Å
Structure data

21018

6v1x

EMDB-21018, PDB-6v1x:
Cryo-EM Structure of the Hyperpolarization-Activated Potassium Channel KAT1: Tetramer
Method: EM (single particle) / Resolution: 3.5 Å

21019

6v1y

EMDB-21019, PDB-6v1y:
Cryo-EM Structure of the Hyperpolarization-Activated Potassium Channel KAT1: Octamer
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-QNP:
(2S)-1-(nonanoyloxy)-3-(phosphonooxy)propan-2-yl tetradecanoate

ChemComp-QNJ:
(3beta,5beta,14beta,17alpha)-cholestan-3-ol

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSPORT PROTEIN / membrane protein / voltage-gated ion channel / potassium channel

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