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.
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2021-01-01
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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. |
first_indexed | 2024-12-19T04:06:15Z |
format | Article |
id | doaj.art-db0829dbaea348d0bf08d38e1f44870d |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-19T04:06:15Z |
publishDate | 2021-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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