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

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.

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2021-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-20468-7
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author 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
author_facet 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
author_sort Alexander A. Shcherbakov
collection DOAJ
description 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.
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spelling doaj.art-db0829dbaea348d0bf08d38e1f44870d2022-12-21T20:36:31ZengNature PortfolioNature Communications2041-17232021-01-0112111310.1038/s41467-020-20468-7Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayersAlexander A. Shcherbakov0Grant Hisao1Venkata S. Mandala2Nathan E. Thomas3Mohammad Soltani4E. A. Salter5James H. Davis6Katherine A. Henzler-Wildman7Mei Hong8Department of Chemistry, Massachusetts Institute of TechnologyDepartment of Biochemistry, University of Wisconsin at MadisonDepartment of Chemistry, Massachusetts Institute of TechnologyDepartment of Biochemistry, University of Wisconsin at MadisonDepartment of Chemistry, University of South AlabamaDepartment of Chemistry, University of South AlabamaDepartment of Chemistry, University of South AlabamaDepartment of Biochemistry, University of Wisconsin at MadisonDepartment of Chemistry, Massachusetts Institute of TechnologyThe 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.https://doi.org/10.1038/s41467-020-20468-7
spellingShingle 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
Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers
Nature Communications
title Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers
title_full Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers
title_fullStr Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers
title_full_unstemmed Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers
title_short Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers
title_sort structure and dynamics of the drug bound bacterial transporter emre in lipid bilayers
url https://doi.org/10.1038/s41467-020-20468-7
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