Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6EBM

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha

Summary for 6EBM
Entry DOI10.2210/pdb6ebm/pdb
EMDB information9024 9025 9026
DescriptorPotassium voltage-gated channel subfamily A member 2,Potassium voltage-gated channel subfamily B member 2 chimera (1 entity in total)
Functional Keywordsmembrane protein, transport protein, potassium channel, lipid nanodisc
Biological sourceRattus norvegicus (Rat)
More
Total number of polymer chains4
Total formula weight235623.31
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 citationMatthies, 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: 30109985
DOI: 10.7554/eLife.37558
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

243083

数据于2025-10-15公开中

PDB statisticsPDBj update infoContact PDBjnumon