ArticleNature2016
Structural insight into the role of the Ton complex in energy transduction.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 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.
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Who cites it
91 citing papers in PubMed, 183 citations in OpenAlex.
- Targeting Ferroptosis and Cuproptosis for Antimicrobial Control in Postharvest Preservation.Comprehensive reviews in food science and food safety · 2026Review
- Multiple TonB-dependent transport systems inInfection and immunity · 2026Article
- The transcriptional repressor PheR regulates uptake and catabolism of phenanthrene in Sphingobium sp. SHPJ-2.The Journal of biological chemistry · 2026Article
- Structural basis of outer membrane biogenesis and cell division by Tol/Pal nanomachinery.Science advances · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Deletion ofApplied and environmental microbiology · 2026Article
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- An RNA sponge directs the transition from feast to famine in Caulobacter crescentus.Nature communications · 2025Article
- Stringent response-mediated ferroptosis-like death resistance underliesApplied and environmental microbiology · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- High-affinity PQQ import is widespread in Gram-negative bacteria.Science advances · 2025Article
- Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogenScience advances · 2025Article
- Primary role of the Tol-Pal complex in bacterial outer membrane lipid homeostasis.Nature communications · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Transcriptome analysis ofFrontiers in microbiology · 2025Article
- Bacterial siderophores: diversity, uptake pathways and applications.Nature reviews. Microbiology · 2025Review
- The Tol Pal system integrates maintenance of the three layered cell envelope.npj antimicrobials and resistance · 2024Review
31 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 7 institutions in 4 countries.
Funding
Abstract
In Gram-negative bacteria, outer membrane transporters import nutrients by coupling to an inner membrane protein complex called the Ton complex. The Ton complex consists of TonB, ExbB, and ExbD, and uses the proton motive force at the inner membrane to transduce energy to the outer membrane via TonB. Here, we structurally characterize the Ton complex from Escherichia coli using X-ray crystallography, electron microscopy, double electron-electron resonance (DEER) spectroscopy, and crosslinking. Our results reveal a stoichiometry consisting of a pentamer of ExbB, a dimer of ExbD, and at least one TonB. Electrophysiology studies show that the Ton subcomplex forms pH-sensitive cation-selective channels and provide insight into the mechanism by which it may harness the proton motive force to produce energy.
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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.