5TJ6
Ca2+ bound aplysia Slo1
Summary for 5TJ6
| Entry DOI | 10.2210/pdb5tj6/pdb |
| Related | 5JTI |
| EMDB information | 8410 8414 |
| Descriptor | High conductance calcium-activated potassium channel, POTASSIUM ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | ion channel, k+ channel, ca2+ bound, high conductance, membrane protein |
| Biological source | Aplysia californica (California sea hare) |
| Total number of polymer chains | 1 |
| Total formula weight | 131843.06 |
| Authors | MacKinnon, R.,Tao, X.,Hite, R.K. (deposition date: 2016-10-03, release date: 2016-12-14, Last modification date: 2024-03-13) |
| Primary citation | Tao, X.,Hite, R.K.,MacKinnon, R. Cryo-EM structure of the open high-conductance Ca(2+)-activated K(+) channel. Nature, 541:46-51, 2017 Cited by 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 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. PubMed: 27974795DOI: 10.1038/nature20608 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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