8GH9
Cryo-EM structure of hSlo1 in total membrane vesicles
Summary for 8GH9
| Entry DOI | 10.2210/pdb8gh9/pdb |
| EMDB information | 40038 40044 40045 |
| Descriptor | Calcium-activated potassium channel subunit alpha-1 (1 entity in total) |
| Functional Keywords | slo1, bk channel, ca2+- and voltage-activated k+ channel, ion channel, toal cell membrane vesicles, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 483632.50 |
| Authors | Tao, X.,Zhao, C.,MacKinnon, R. (deposition date: 2023-03-09, release date: 2023-05-10, Last modification date: 2024-06-19) |
| Primary citation | Tao, X.,Zhao, C.,MacKinnon, R. Membrane protein isolation and structure determination in cell-derived membrane vesicles. Proc.Natl.Acad.Sci.USA, 120:e2302325120-e2302325120, 2023 Cited by PubMed Abstract: Integral membrane protein structure determination traditionally requires extraction from cell membranes using detergents or polymers. Here, we describe the isolation and structure determination of proteins in membrane vesicles derived directly from cells. Structures of the ion channel Slo1 from total cell membranes and from cell plasma membranes were determined at 3.8 Å and 2.7 Å resolution, respectively. The plasma membrane environment stabilizes Slo1, revealing an alteration of global helical packing, polar lipid, and cholesterol interactions that stabilize previously unresolved regions of the channel and an additional ion binding site in the Ca regulatory domain. The two methods presented enable structural analysis of both internal and plasma membrane proteins without disrupting weakly interacting proteins, lipids, and cofactors that are essential to biological function. PubMed: 37098056DOI: 10.1073/pnas.2302325120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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