6EBM
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha
Summary for 6EBM
Entry DOI | 10.2210/pdb6ebm/pdb |
EMDB information | 9024 9025 9026 |
Descriptor | Potassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B member 2 chimera (1 entity in total) |
Functional Keywords | membrane protein, transport protein, potassium channel, lipid nanodisc |
Biological source | Rattus norvegicus (Rat) More |
Total number of polymer chains | 4 |
Total formula weight | 235623.31 |
Authors | Matthies, D.,Bae, C.,Fox, T.,Bartesaghi, A.,Subramaniam, S.,Swartz, K.J. (deposition date: 2018-08-06, release date: 2018-08-22, Last modification date: 2024-03-13) |
Primary citation | Matthies, D.,Bae, C.,Toombes, G.E.,Fox, T.,Bartesaghi, A.,Subramaniam, S.,Swartz, K.J. Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs. Elife, 7:-, 2018 Cited by PubMed Abstract: Voltage-activated potassium (Kv) channels open to conduct K ions in response to membrane depolarization, and subsequently enter non-conducting states through distinct mechanisms of inactivation. X-ray structures of detergent-solubilized Kv channels appear to have captured an open state even though a non-conducting C-type inactivated state would predominate in membranes in the absence of a transmembrane voltage. However, structures for a voltage-activated ion channel in a lipid bilayer environment have not yet been reported. Here we report the structure of the Kv1.2-2.1 paddle chimera channel reconstituted into lipid nanodiscs using single-particle cryo-electron microscopy. At a resolution of ~3 Å for the cytosolic domain and ~4 Å for the transmembrane domain, the structure determined in nanodiscs is similar to the previously determined X-ray structure. Our findings show that large differences in structure between detergent and lipid bilayer environments are unlikely, and enable us to propose possible structural mechanisms for C-type inactivation. PubMed: 30109985DOI: 10.7554/eLife.37558 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
Download full validation report
