Voltage sensor dynamics of a bacterial voltage-gated sodium channel NavAb reveal three conformational states.
Ontology highlight
ABSTRACT: High-resolution structures of voltage-gated sodium channels (Nav) were first obtained from a prokaryotic ortholog NavAb, which provided important mechanistic insights into Na+ selectivity and voltage gating. Unlike eukaryotic Navs, the NavAb channel is formed by four identical subunits, but its ion selectivity and pharmacological profiles are very similar to eukaryotic Navs. Recently, the structures of the NavAb voltage sensor at resting and activated states were obtained by cryo-EM, but its intermediate states and transition dynamics remain unclear. In the present work, we used liposome flux assays to show that purified NavAb proteins were functional to conduct both H+ and Na+ and were blocked by the local anesthetic lidocaine. Additionally, we examined th
SUBMITTER: Han S
PROVIDER: S-EPMC9986516 | biostudies-literature | 2023 Feb
REPOSITORIES: biostudies-literature
ACCESS DATA