The Multidrug Transporter MdfA Deviates from the Canonical Model of Alternating Access of MFS Transporters.

ABSTRACT: The prototypic multidrug (Mdr) transporter MdfA from Escherichia coli efflux chemically- dissimilar substrates in exchange for protons. Similar to other transporters, MdfA purportedly functions by alternating access of a central substrate binding pocket to either side of the membrane. Accordingly, MdfA should open at the cytoplasmic side and/or laterally toward the membrane to enable access of drugs into its pocket. At the end of the cycle, the periplasmic side is expected to open to release drugs. Two distinct conformations of MdfA have been captured by X-ray crystallography: An outward open (O_o) conformation, stabilized by a Fab fragment, and a ligand-bound inward-facing (I_f) conformation, possibly stabilized by a mutation (Q131R). Here, we investigated how these st

SUBMITTER: Yardeni EH 

PROVIDER: S-EPMC7541688 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature