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Membrane Chemistry Tunes the Structure of a Peptide Transporter
Membrane proteins require lipid bilayers for function. While lipid compositions reach enormous complexities, high‐resolution structures are usually obtained in artificial detergents. To understand whether and how lipids guide membrane protein function, we use single‐molecule FRET to probe the dynami...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7590137/ https://www.ncbi.nlm.nih.gov/pubmed/32744783 http://dx.doi.org/10.1002/anie.202008226 |
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author | Lasitza‐Male, Tanya Bartels, Kim Jungwirth, Jakub Wiggers, Felix Rosenblum, Gabriel Hofmann, Hagen Löw, Christian |
author_facet | Lasitza‐Male, Tanya Bartels, Kim Jungwirth, Jakub Wiggers, Felix Rosenblum, Gabriel Hofmann, Hagen Löw, Christian |
author_sort | Lasitza‐Male, Tanya |
collection | PubMed |
description | Membrane proteins require lipid bilayers for function. While lipid compositions reach enormous complexities, high‐resolution structures are usually obtained in artificial detergents. To understand whether and how lipids guide membrane protein function, we use single‐molecule FRET to probe the dynamics of DtpA, a member of the proton‐coupled oligopeptide transporter (POT) family, in various lipid environments. We show that detergents trap DtpA in a dynamic ensemble with cytoplasmic opening. Only reconstitutions in more native environments restore cooperativity, allowing an opening to the extracellular side and a sampling of all relevant states. Bilayer compositions tune the abundance of these states. A novel state with an extreme cytoplasmic opening is accessible in bilayers with anionic head groups. Hence, chemical diversity of membranes translates into structural diversity, with the current POT structures only sampling a portion of the full structural space. |
format | Online Article Text |
id | pubmed-7590137 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-75901372020-10-30 Membrane Chemistry Tunes the Structure of a Peptide Transporter Lasitza‐Male, Tanya Bartels, Kim Jungwirth, Jakub Wiggers, Felix Rosenblum, Gabriel Hofmann, Hagen Löw, Christian Angew Chem Int Ed Engl Research Articles Membrane proteins require lipid bilayers for function. While lipid compositions reach enormous complexities, high‐resolution structures are usually obtained in artificial detergents. To understand whether and how lipids guide membrane protein function, we use single‐molecule FRET to probe the dynamics of DtpA, a member of the proton‐coupled oligopeptide transporter (POT) family, in various lipid environments. We show that detergents trap DtpA in a dynamic ensemble with cytoplasmic opening. Only reconstitutions in more native environments restore cooperativity, allowing an opening to the extracellular side and a sampling of all relevant states. Bilayer compositions tune the abundance of these states. A novel state with an extreme cytoplasmic opening is accessible in bilayers with anionic head groups. Hence, chemical diversity of membranes translates into structural diversity, with the current POT structures only sampling a portion of the full structural space. John Wiley and Sons Inc. 2020-09-11 2020-10-19 /pmc/articles/PMC7590137/ /pubmed/32744783 http://dx.doi.org/10.1002/anie.202008226 Text en © 2020 The Authors. Published by Wiley-VCH GmbH This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Lasitza‐Male, Tanya Bartels, Kim Jungwirth, Jakub Wiggers, Felix Rosenblum, Gabriel Hofmann, Hagen Löw, Christian Membrane Chemistry Tunes the Structure of a Peptide Transporter |
title | Membrane Chemistry Tunes the Structure of a Peptide Transporter
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title_full | Membrane Chemistry Tunes the Structure of a Peptide Transporter
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title_fullStr | Membrane Chemistry Tunes the Structure of a Peptide Transporter
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title_full_unstemmed | Membrane Chemistry Tunes the Structure of a Peptide Transporter
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title_short | Membrane Chemistry Tunes the Structure of a Peptide Transporter
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title_sort | membrane chemistry tunes the structure of a peptide transporter |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7590137/ https://www.ncbi.nlm.nih.gov/pubmed/32744783 http://dx.doi.org/10.1002/anie.202008226 |
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