Conformation space of a heterodimeric ABC exporter under turnover conditions.

ABSTRACT: Cryo-electron microscopy (cryo-EM) has the capacity to capture molecular machines in action^1-3. ATP-binding cassette (ABC) exporters are highly dynamic membrane proteins that extrude a wide range of substances from the cytosol^4-6 and thereby contribute to essential cellular processes, adaptive immunity and multidrug resistance^7,8. Despite their importance, the coupling of nucleotide binding, hydrolysis and release to the conformational dynamics of these proteins remains poorly resolved, especially for heterodimeric and/or asymmetric ABC exporters that are abundant in humans. Here we present eight high-resolution cryo-EM structures that delineate the full functional cycle of an asymmetric ABC exporter in a lipid environment. Cryo-EM analysis under active tur

SUBMITTER: Hofmann S 

PROVIDER: S-EPMC7612745 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature