Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 43, Pages 19121-19128Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202008226
Keywords
FRET; biomembranes; membrane proteins; protein structures; single-molecule studies
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Funding
- German-Israeli Foundation (GIF) [G-1288207.9/2015]
- Projekt DEAL
- Benoziyo Fund for the Advancement of Science
- Gurwin Family Fund for Scientific Research
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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.
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