ArticleCommunications biology2019
Cryo-EM structure of the bacterial Ton motor subcomplex ExbB-ExbD provides information on structure and stoichiometry.
Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers.
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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
44 citing papers in PubMed.
- Identification of a Putative Metal Transporter in the Apicoplast of Malaria Parasites.bioRxiv : the preprint server for biology · 2026Article
- Modulating backbone flexibility in hydroxamate siderophores for improved iron chelation and peptide nucleic acid delivery into bacteria.The Biochemical journal · 2026Article
- Bacterial Siderophore Production in Metal-Rich Environments: Underexplored Sources of Siderophores and Insights into Bioremediation.Journal of natural products · 2026Review
- Structural basis of outer membrane biogenesis and cell division by Tol/Pal nanomachinery.Science advances · 2026Article
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- Article
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- Origin and Evolution of Bacterial Periplasmic Force Transducers.Molecular biology and evolution · 2025Article
- Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogenScience advances · 2025Article
- Bacterial siderophores: diversity, uptake pathways and applications.Nature reviews. Microbiology · 2025Review
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- The role of FoxA, FiuA, and FpvB in iron acquisition via hydroxamate-type siderophores in Pseudomonas aeruginosa.Scientific reports · 2024Article
- Whole-Cell Biosensor for Iron Monitoring as a Potential Tool for Safeguarding Biodiversity in Polar Marine Environments.Marine drugs · 2024Review
- Assimilation of phthalate esters in bacteria.Applied microbiology and biotechnology · 2024Review
- Siderophores as tools and treatments.npj antimicrobials and resistance · 2024Review
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Experimental and computational methods to highlight behavioural variations in TonB-dependent transporter expression in Pseudomonas aeruginosa versus siderophore concentration.Scientific reports · 2023Article
- Energization of Outer Membrane Transport by the ExbB ExbD Molecular Motor.Journal of bacteriology · 2023Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors.
Funding
Abstract
The TonB-ExbB-ExbD molecular motor harnesses the proton motive force across the bacterial inner membrane to couple energy to transporters at the outer membrane, facilitating uptake of essential nutrients such as iron and cobalamine. TonB physically interacts with the nutrient-loaded transporter to exert a force that opens an import pathway across the outer membrane. Until recently, no high-resolution structural information was available for this unique molecular motor. We published the first crystal structure of ExbB-ExbD in 2016 and showed that five copies of ExbB are arranged as a pentamer around a single copy of ExbD. However, our spectroscopic experiments clearly indicated that two copies of ExbD are present in the complex. To resolve this ambiguity, we used single-particle cryo-electron microscopy to show that the ExbB pentamer encloses a dimer of ExbD in its transmembrane pore, and not a monomer as previously reported. The revised stoichiometry has implications for motor function.
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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.