ArticleNature communications2023
Expulsion mechanism of the substrate-translocating subunit in ECF transporters.
Article in Nature communications, 2023. 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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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- Targeting the Energy-Coupling Factor Transporters: A Novel Antibiotic Drug Target inJournal of medicinal chemistry · 2026Article
- Bridging Scales: Coarse-Grained Protein Models in Computational Biology.Advances in experimental medicine and biology · 2026Review
- The Martini 3 Lipidome: Expanded and Refined Parameters Improve Lipid Phase Behavior.ACS central science · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Single-molecule visualization of ATP-induced dynamics of the subunit composition of an ECF transporter complex under turnover conditions.Nature communications · 2025Article
- In Vitro Antimicrobial Efficacy Assessment of Ethanolic, Aqueous, and Dual Solvent Extracts of MushroomAntibiotics (Basel, Switzerland) · 2024Article
- Expression and characterization of pantothenate energy-coupling factor transporters as an anti-infective drug target.Protein science : a publication of the Protein Society · 2024Article
- Coenzyme A biosynthesis inmBio · 2024Article
- The S-component fold: a link between bacterial transporters and receptors.Communications biology · 2024Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF module) Previous data indicate that the S-component topples within the membrane to alternately expose the binding site to either side of the membrane. In many ECF transporters, the substrate-free S-component can be expelled from the ECF module. Here we study this enigmatic expulsion step by cryogenic electron microscopy and reveal that ATP induces a concave-to-convex shape change of two long helices in the motor, thereby destroying the S-component's docking site and allowing for its dissociation. We show that adaptation of the membrane morphology to the conformational state of the motor may favour expulsion of the substrate-free S-component when ATP is bound and docking of the substrate-loaded S-component after hydrolysis. Our work provides a picture of bilayer-assisted chemo-mechanical coupling in the transport cycle of ECF transporters.
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