ArticleNature communications2025
Cryo-EM structures of the E. coli Ton and Tol motor complexes.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Multiple TonB-dependent transport systems inInfection and immunity · 2026Article
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Receptor-substrate competition for the TonB homolog FusB suggests a model for ferredoxin import.The Journal of biological chemistry · 2026Article
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Breaking the outer membrane barrier: structure, targets, and antimicrobial strategies for Gram-negative bacteria.Frontiers in microbiology · 2026Review
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- Origin and Evolution of Bacterial Periplasmic Force Transducers.Molecular biology and evolution · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The Ton and Tol motor proteins use the proton gradient at the inner membrane of Gram-negative bacteria as an energy source. The generated force is transmitted through the periplasmic space to protein components associated with the outer membrane, either to maintain the outer membrane integrity for the Tol system, or to allow essential nutrients to enter the cell for Ton. We have solved the high-resolution structures of the E. coli TonB-ExbB-ExbD and TolA-TolQ-TolR complexes, revealing the inner membrane embedded engine parts of the Ton and Tol systems, and showing how TonB and TolA interact with the ExbBD and TolQR subcomplexes. Structural similarities between the two motor complexes suggest a common mechanism for the opening of the proton channel and the propagation of the proton motive force into movement of the TonB and TolA subunits. Because TonB and TolA bind at preferential ExbB or TolQ subunits, we propose a new mechanism of assembly of TonB and TolA with their respective ExbBD and TolQR subcomplexes and discuss its impact on the mechanism of action for the Ton and Tol systems.
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What Socratic 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 Socratic graph.