6V38
Cryo-EM structure of Ca2+-bound hsSlo1 channel
Summary for 6V38
| Entry DOI | 10.2210/pdb6v38/pdb |
| Related | 6V22 |
| EMDB information | 21025 21028 21029 21036 |
| Descriptor | Calcium-activated potassium channel subunit alpha-1, MAGNESIUM ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | high conductance ca2+-activated k+ channel, slo1 channel, bk channel, maxik channel, transport protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 509332.37 |
| Authors | Tao, X.,MacKinnon, R. (deposition date: 2019-11-25, release date: 2019-12-25, Last modification date: 2024-03-06) |
| Primary citation | Tao, X.,MacKinnon, R. Molecular structures of the human Slo1 K + channel in complex with beta 4. Elife, 8:-, 2019 Cited by PubMed Abstract: Slo1 is a Ca- and voltage-activated K channel that underlies skeletal and smooth muscle contraction, audition, hormone secretion and neurotransmitter release. In mammals, Slo1 is regulated by auxiliary proteins that confer tissue-specific gating and pharmacological properties. This study presents cryo-EM structures of Slo1 in complex with the auxiliary protein, β4. Four β4, each containing two transmembrane helices, encircle Slo1, contacting it through helical interactions inside the membrane. On the extracellular side, β4 forms a tetrameric crown over the pore. Structures with high and low Ca concentrations show that identical gating conformations occur in the absence and presence of β4, implying that β4 serves to modulate the relative stabilities of 'pre-existing' conformations rather than creating new ones. The effects of β4 on scorpion toxin inhibition kinetics are explained by the crown, which constrains access but does not prevent binding. PubMed: 31815672DOI: 10.7554/eLife.51409 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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