Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers

Alexander A. Shcherbakov; Grant Hisao; Venkata S. Mandala; Nathan E. Thomas; Mohammad Soltani; E. A. Salter; James H. Davis; Katherine A. Henzler-Wildman; Mei Hong

doi:10.1038/s41467-020-20468-7

Nature Communications (Jan 2021)

Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers

Alexander A. Shcherbakov,
Grant Hisao,
Venkata S. Mandala,
Nathan E. Thomas,
Mohammad Soltani,
E. A. Salter,
James H. Davis,
Katherine A. Henzler-Wildman,
Mei Hong

Affiliations

Alexander A. Shcherbakov: Department of Chemistry, Massachusetts Institute of Technology
Grant Hisao: Department of Biochemistry, University of Wisconsin at Madison
Venkata S. Mandala: Department of Chemistry, Massachusetts Institute of Technology
Nathan E. Thomas: Department of Biochemistry, University of Wisconsin at Madison
Mohammad Soltani: Department of Chemistry, University of South Alabama
E. A. Salter: Department of Chemistry, University of South Alabama
James H. Davis: Department of Chemistry, University of South Alabama
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/s41467-020-20468-7
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 13

Abstract

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The small proton-coupled transporter EmrE confers multidrug resistance in bacteria. The structure of drug-bound EmrE in phospholipid bilayers is now determined using solid-state NMR. The structure provides detailed insights into the molecular mechanism of substrate recognition by this transporter.

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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