Electrostatic lock in the transport cycle of the multidrug resistance transporter EmrE.

ABSTRACT: EmrE is a small, homodimeric membrane transporter that exploits the established electrochemical proton gradient across the Escherichia coli inner membrane to export toxic polyaromatic cations, prototypical of the wider small-multidrug resistance transporter family. While prior studies have established many fundamental aspects of the specificity and rate of substrate transport in EmrE, low resolution of available structures has hampered identification of the transport coupling mechanism. Here we present a complete, refined atomic structure of EmrE optimized against available cryo-electron microscopy (cryo-EM) data to delineate the critical interactions by which EmrE regulates its conformation during the transport process. With the model, we conduct molecular dynamics simulations of t

SUBMITTER: Vermaas JV 

PROVIDER: S-EPMC6094130 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature