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

Alexander A. Shcherbakov; Peyton J. Spreacker; Aurelio J. Dregni; Katherine A. Henzler-Wildman; Mei Hong

doi:10.1038/s41467-022-28556-6

Nature Communications (Feb 2022)

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

Alexander A. Shcherbakov,
Peyton J. Spreacker,
Aurelio J. Dregni,
Katherine A. Henzler-Wildman,
Mei Hong

Affiliations

Alexander A. Shcherbakov: Department of Chemistry, Massachusetts Institute of Technology
Peyton J. Spreacker: Department of Biochemistry, University of Wisconsin at Madison
Aurelio J. Dregni: Department of Chemistry, Massachusetts Institute of Technology
Katherine A. Henzler-Wildman: Department of Biochemistry, University of Wisconsin at Madison
Mei Hong: Department of Chemistry, Massachusetts Institute of Technology

DOI: https://doi.org/10.1038/s41467-022-28556-6
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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EmrE transporter effluxes cationic substrates across lipid membranes in a pH-coupled manner. Here, the authors solve the structure of ligand-bound EmrE at high pH by NMR, with insights into the transport mechanism.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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