ArticleProceedings of the National Academy of Sciences of the United States of America2021
Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 13 citations in OpenAlex.
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters.Nature communications · 2026Article
- Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Repurposing antimalarials: pyrimethamine exhibits superior in vitro activity to metronidazole against Gardnerella while sparing Lactobacillus.The Journal of antimicrobial chemotherapy · 2025Article
- Single-molecule visualization of ATP-induced dynamics of the subunit composition of an ECF transporter complex under turnover conditions.Nature communications · 2025Article
- MreC-MreD structure reveals a multifaceted interface that controls MreC conformation.bioRxiv : the preprint server for biology · 2024Article
- The S-component fold: a link between bacterial transporters and receptors.Communications biology · 2024Article
- Bidirectional ATP-driven transport of cobalamin by the mycobacterial ABC transporter BacA.Nature communications · 2024Article
- Identification of inhibitors targeting the energy-coupling factor (ECF) transporters.Communications biology · 2023Article
- Expulsion mechanism of the substrate-translocating subunit in ECF transporters.Nature communications · 2023Article
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4 authors at 1 institution in 1 country.
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Abstract
Energy-coupling factor (ECF)-type transporters are small, asymmetric membrane protein complexes (∼115 kDa) that consist of a membrane-embedded, substrate-binding protein (S component) and a tripartite ATP-hydrolyzing module (ECF module). They import micronutrients into bacterial cells and have been proposed to use a highly unusual transport mechanism, in which the substrate is dragged across the membrane by a toppling motion of the S component. However, it remains unclear how the lipid bilayer could accommodate such a movement. Here, we used cryogenic electron microscopy at 200 kV to determine structures of a folate-specific ECF transporter in lipid nanodiscs and detergent micelles at 2.7- and 3.4-Å resolution, respectively. The structures reveal an irregularly shaped bilayer environment around the membrane-embedded complex and suggest that toppling of the S component is facilitated by protein-induced membrane deformations. In this way, structural remodeling of the lipid bilayer environment is exploited to guide the transport process.
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