ArticleNature communications2016
Structural insight in the toppling mechanism of an energy-coupling factor transporter.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 59 citations in OpenAlex.
- Targeting the Energy-Coupling Factor Transporters: A Novel Antibiotic Drug Target inJournal of medicinal chemistry · 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
- Single-molecule visualization of ATP-induced dynamics of the subunit composition of an ECF transporter complex under turnover conditions.Nature communications · 2025Article
- Improved methyl supply for 5-methyltetrahydrofolate production in E. coli through a novel C1 transfer pathway.Microbial cell factories · 2025Article
- Expression and characterization of pantothenate energy-coupling factor transporters as an anti-infective drug target.Protein science : a publication of the Protein Society · 2024Article
- 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
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
- Expulsion mechanism of the substrate-translocating subunit in ECF transporters.Nature communications · 2023Article
- Article
- Structure-Guided Optimization of Small-Molecule Folate Uptake Inhibitors Targeting the Energy-Coupling Factor Transporters.Journal of medicinal chemistry · 2022Article
- Review
- Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Role of the Membrane in Transporter Folding and Activity.Journal of molecular biology · 2021Review
- Structural and biophysical characterization of the tandem substrate-binding domains of the ABC importer GlnPQ.Open biology · 2021Article
- Article
- Characterization of the Streptococcus mutansJournal of bacteriology · 2020Article
- Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Energy-coupling factor (ECF) transporters mediate uptake of micronutrients in prokaryotes. The transporters consist of an S-component that binds the transported substrate and an ECF module (EcfAA'T) that binds and hydrolyses ATP. The mechanism of transport is poorly understood but presumably involves an unusual step in which the membrane-embedded S-component topples over to carry the substrate across the membrane. In many ECF transporters, the S-component dissociates from the ECF module after transport. Subsequently, substrate-bound S-components out-compete the empty proteins for re-binding to the ECF module in a new round of transport. Here we present crystal structures of the folate-specific transporter ECF-FolT from Lactobacillus delbrueckii. Interaction of the ECF module with FolT stabilizes the toppled state, and simultaneously destroys the high-affinity folate-binding site, allowing substrate release into the cytosol. We hypothesize that differences in the kinetics of toppling can explain how substrate-loaded FolT out-competes apo-FolT for association with the ECF module.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.