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TitleSingle-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs.
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateAug 15, 2018
AuthorsDoreen Matthies / Chanhyung Bae / Gilman Es Toombes / Tara Fox / Alberto Bartesaghi / Sriram Subramaniam / Kenton Jon Swartz /
PubMed AbstractVoltage-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- ...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.
External linksElife / PubMed:30109985 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 4.0 Å
Structure data

EMDB-9024, PDB-6ebk:
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-9025, PDB-6ebl:
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic domain
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-9026, PDB-6ebm:
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

ChemComp-HOH:
WATER / Water

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / transport protein / potassium channel / lipid nanodisc

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