ArticleThe Journal of biological chemistry2007
Evidence of ball-and-chain transport of ferric enterobactin through FepA.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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
35 citing papers in PubMed, 85 citations in OpenAlex.
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Siderophore-mediated iron acquisition byJournal of bacteriology · 2024Article
- Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu.Frontiers in microbiology · 2024Article
- Siderophores as tools and treatments.npj antimicrobials and resistance · 2024Review
- The occurrence, characteristics, and adaptation of A-to-I RNA editing in bacteria: A review.Frontiers in microbiology · 2023Review
- Fluorescent Binding Protein Sensors for Detection and Quantification of Biochemicals, Metabolites, and Natural Products.Bio-protocol · 2022Article
- A-to-I mRNA Editing in a Ferric Siderophore Receptor Improves Competition for Iron in Xanthomonas oryzae pv.Microbiology spectrum · 2021Article
- Article
- Biomimetic enterobactin analogue mediates iron-uptake and cargo transport intoChemical science · 2021Article
- Conformational rearrangements in the N-domain ofThe Journal of biological chemistry · 2020Article
- Universal fluorescent sensors of high-affinity iron transport, applied to ESKAPE pathogens.The Journal of biological chemistry · 2019Article
- Fluorescence High-Throughput Screening for Inhibitors of TonB Action.Journal of bacteriology · 2017Article
- Ligand Induced Conformational Changes of a Membrane Transporter in E. coli Cells Observed with DEER/PELDOR.Journal of the American Chemical Society · 2016Article
- ROSET Model of TonB Action in Gram-Negative Bacterial Iron Acquisition.Journal of bacteriology · 2016Review
- Article
- Iron and zinc exploitation during bacterial pathogenesis.Metallomics : integrated biometal science · 2015Review
- Concerted loop motion triggers induced fit of FepA to ferric enterobactin.The Journal of general physiology · 2014Article
- Energy-dependent motion of TonB in the Gram-negative bacterial inner membrane.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Use of a molecular decoy to segregate transport from antigenicity in the FrpB iron transporter from Neisseria meningitidis.PloS one · 2013Article
- TonB-dependent transporter FhuA in planar lipid bilayers: partial exit of its plug from the barrel.Biochemistry · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
The Escherichia coli iron transporter, FepA, has a globular N terminus that resides within a transmembrane beta-barrel formed by its C terminus. We engineered 25 cysteine substitution mutations at different locations in FepA and modified their sulfhydryl side chains with fluorescein maleimide in live cells. The reactivity of the Cys residues changed, sometimes dramatically, during the transport of ferric enterobactin, the natural ligand of FepA. Patterns of Cys susceptibility reflected energy- and TonB-dependent motion in the receptor protein. During transport, a residue on the normally buried surface of the N-domain was labeled by fluorescein maleimide in the periplasm, providing evidence that the transport process involves expulsion of the globular domain from the beta-barrel. Porin deficiency much reduced the fluoresceination of this site, confirming the periplasmic labeling route. These data support the previously proposed, but never demonstrated, ball-and-chain theory of membrane transport. Functional complementation between a separately expressed N terminus and C-terminal beta-barrel domain confirmed the feasibility of this mechanism.
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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.