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| Title | Cryo-EM structure of the open high-conductance Ca-activated K channel. |
|---|---|
| Journal, issue, pages | Nature, Vol. 541, Issue 7635, Page 46-51, Year 2017 |
| Publish date | Jan 5, 2017 |
 Authors | Xiao Tao / Richard K Hite / Roderick MacKinnon /  |
| PubMed Abstract | The Ca-activated K channel, Slo1, has an unusually large conductance and contains a voltage sensor and multiple chemical sensors. Dual activation by membrane voltage and Ca renders Slo1 central to ...The Ca-activated K channel, Slo1, has an unusually large conductance and contains a voltage sensor and multiple chemical sensors. Dual activation by membrane voltage and Ca renders Slo1 central to processes that couple electrical signalling to Ca-mediated events such as muscle contraction and neuronal excitability. Here we present the cryo-electron microscopy structure of a full-length Slo1 channel from Aplysia californica in the presence of Ca and Mg at a resolution of 3.5 Å. The channel adopts an open conformation. Its voltage-sensor domain adopts a non-domain-swapped attachment to the pore and contacts the cytoplasmic Ca-binding domain from a neighbouring subunit. Unique structural features of the Slo1 voltage sensor suggest that it undergoes different conformational changes than other known voltage sensors. The structure reveals the molecular details of three distinct divalent cation-binding sites identified through electrophysiological studies of mutant Slo1 channels. |
 External links | Nature / PubMed:27974795 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.5 Å |
| Structure data | |
| Chemicals |  ChemComp-K:  ChemComp-MG:  ChemComp-CA:  ChemComp-PGW: |
| Source |
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 Keywords |  MEMBRANE PROTEIN / ion channel / K+ channel / Ca2+ bound / high conductance |
