High structure of EmrE reveals the mechanism of proton-coupled substrate transport

AA Shcherbakov, PJ Spreacker, AJ Dregni, Katherine A. Henzler-Wildman, https://doi.org/10.1038/s41467-022-28556-6 Mei Hong
Nat Commun 13, 991 (2022).
Science Published: (Feb/2022)
DOI: https://doi.org/10.1038/s41467-022-28556-6

The homo-dimeric bacterial membrane protein EmrE effluxes polyaromatic cationic substrates in a proton-coupled manner to cause multidrug resistance. We recently determined the structure of substrate-bound EmrE in phospholipid bilayers by measuring hundreds of protein-ligand HN–F distances for a fluorinated substrate, 4-fluoro-tetraphenylphosphonium (F 4-TPP+), using solid-state NMR. This structure was solved at low pH where one of the two proton-binding Glu14 residues is …

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