Structure of the EmrE multidrug transporter and its use for inhibitor peptide design.

ABSTRACT: Small multidrug resistance (SMR) pumps represent a minimal paradigm of proton-coupled membrane transport in bacteria, yet no high-resolution structure of an SMR protein is available. Here, atomic-resolution structures of the Escherichia coli efflux-multidrug resistance E (EmrE) multidrug transporter in ligand-bound form are refined using microsecond molecular dynamics simulations biased using low-resolution data from X-ray crystallography. The structures are compatible with existing mutagenesis data as well as NMR and biochemical experiments, including pKas of the catalytic glutamate residues and the dissociation constant ([Formula: see text]) of the tetraphenylphosphonium⁺ cation. The refined structures show the arrangement of residue side chains in the EmrE

SUBMITTER: Ovchinnikov V 

PROVIDER: S-EPMC6112734 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature