5A6E
Cryo-EM structure of the Slo2.2 Na-activated K channel
Summary for 5A6E
| Entry DOI | 10.2210/pdb5a6e/pdb |
| Related | 5A6F 5A6G |
| EMDB information | 3062 |
| Descriptor | S1-S4 DOMAIN OF POTASSIUM CHANNEL SUBFAMILY T MEMBER 1, PORE DOMAIN OF POTASSIUM CHANNEL SUBFAMILY T MEMBER 1, GATING RING OF POTASSIUM CHANNEL SUBFAMILY T MEMBER 1, ... (4 entities in total) |
| Functional Keywords | transport, ion channel, potassium channel |
| Biological source | GALLUS GALLUS (CHICKEN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 105562.06 |
| Authors | Hite, R.K.,Yuan, P.,Li, Z.,Hsuing, Y.,Walz, T.,MacKinnon, R. (deposition date: 2015-06-25, release date: 2015-10-14, Last modification date: 2024-05-08) |
| Primary citation | Hite, R.K.,Yuan, P.,Li, Z.,Hsuing, Y.,Walz, T.,Mackinnon, R. Cryo-Electron Microscopy Structure of the Slo2.2 Na1-Activated K1 Channel Nature, 527:198-, 2015 Cited by PubMed Abstract: Na(+)-activated K(+) channels are members of the Slo family of large conductance K(+) channels that are widely expressed in the brain, where their opening regulates neuronal excitability. These channels fulfil a number of biological roles and have intriguing biophysical properties, including conductance levels that are ten times those of most other K(+) channels and gating sensitivity to intracellular Na(+). Here we present the structure of a complete Na(+)-activated K(+) channel, chicken Slo2.2, in the Na(+)-free state, determined by cryo-electron microscopy at a nominal resolution of 4.5 ångströms. The channel is composed of a large cytoplasmic gating ring, in which resides the Na(+)-binding site and a transmembrane domain that closely resembles voltage-gated K(+) channels. In the structure, the cytoplasmic domain adopts a closed conformation and the ion conduction pore is also closed. The structure reveals features that can explain the unusually high conductance of Slo channels and how contraction of the cytoplasmic gating ring closes the pore. PubMed: 26436452DOI: 10.1038/NATURE14958 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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