ArticleAngewandte Chemie (International ed. in English)2020
Membrane Chemistry Tunes the Structure of a Peptide Transporter.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Model-free photon analysis of diffusion-based single-molecule FRET experiments.Nature communications · 2025Article
- Conformational Landscape of the Di- and Tripeptide Permease A Transport Cycle.Journal of chemical information and modeling · 2025Article
- The conserved lysine residue in transmembrane helix 5 is pivotal for the cytoplasmic gating of the L-amino acid transporters.PNAS nexus · 2025Article
- Functional regulation of aquaporin dynamics by lipid bilayer composition.Nature communications · 2024Article
- Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023Article
- Establishing mammalian GLUT kinetics and lipid composition influences in a reconstituted-liposome system.Nature communications · 2023Article
- Review
- Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes.Science advances · 2021Article
- Diffusion of a disordered protein on its folded ligand.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021Review
- Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins.International journal of molecular sciences · 2021Review
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents.Biochemistry · 2021Article
- Membrane Chemistry Tunes the Structure of a Peptide Transporter.Angewandte Chemie (International ed. in English) · 2020Article
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Authors and funding
7 authors.
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Abstract
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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