Evidence map›Paper›PMID 28429713›Full record

ArticleNature communications2017

Gating of TonB-dependent transporters by substrate-specific forced remodelling.

Samuel J Hickman, Rachael E M Cooper, Luca Bellucci, Emanuele Paci, David J Brockwell

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  9. Article
  10. Cleavage cascade of the sigma regulator FecR orchestrates TonB-dependent signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Proteogenomic Characterization ofMicroorganisms · 2024
    Article
  15. Article
  16. Article
  17. GdJournal of the American Chemical Society · 2023
    Article
  18. Trojan Horse Siderophore Conjugates InduceJournal of medicinal chemistry · 2023
    Article
  19. Article
  20. HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Samuel J HickmanSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Rachael E M CooperSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Luca BellucciNEST, Istituto Nanoscienze-CNR, Piazza San Silvestro, 12-56127 Pisa, Italy.
Emanuele PaciSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
David J BrockwellSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.

Funding

Wellcome Trust
6 · The paper itself

Abstract

Membrane proteins play vital roles in inside-out and outside-in signal transduction by responding to inputs that include mechanical stimuli. Mechanical gating may be mediated by the membrane or by protein(s) but evidence for the latter is scarce. Here we use force spectroscopy, protein engineering and bacterial growth assays to investigate the effects of force on complexes formed between TonB and TonB-dependent transporters (TBDT) from Gram-negative bacteria. We confirm the feasibility of protein-only mediated mechanical gating by demonstrating that the interaction between TonB and BtuB (a TBDT) is sufficiently strong under force to create a channel through the TBDT. In addition, by comparing the dimensions of the force-induced channel in BtuB and a second TBDT (FhuA), we show that the mechanical properties of the interaction are perfectly tuned to their function by inducing formation of a channel whose dimensions are tailored to the ligand.

Indexed as

Ion Channel GatingBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsGram-Negative BacteriaMembrane ProteinsMembrane Transport ProteinsProtein BindingProtein EngineeringSignal TransductionSpectrum AnalysisSubstrate SpecificityBacterial Outer Membrane ProteinsBacterial ProteinsBtuB protein, E coliEscherichia coli ProteinsMembrane ProteinsMembrane Transport ProteinstonB protein, Bacteria

Identifiers

PMID28429713
PMCPMC5413942

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.