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TitleHigh-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport.
Journal, issue, pagesNat Commun, Vol. 13, Page 991-991, Year 2022
Publish dateOct 4, 2021 (structure data deposition date)
AuthorsShcherbakov, A.A. / Spreacker, P.J. / Dregni, A.J. / Henzler-Wildman, K.A. / Hong, M.
External linksNat Commun / PubMed:35181664
MethodsNMR (solid-state)
Structure data

PDB-7sfq:
EmrE S64V Mutant Bound to tetra(4-fluorophenyl)phosphonium at pH 8.0
Method: SOLID-STATE NMR

Chemicals

ChemComp-VCJ:
tetrakis(4-fluorophenyl)phosphanium

Source
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / Multidrug resistance protein / SMR Transporter / Efflux protein / Proton-coupled

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