ReviewJournal of bacteriology2023
Energization of Outer Membrane Transport by the ExbB ExbD Molecular Motor.
Review in Journal of bacteriology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 35 citations in OpenAlex.
- Structural and functional characterisation of the dextran utilisome fromJournal of structural biology: X · 2026Article
- Multiple TonB-dependent transport systems inInfection and immunity · 2026Article
- Receptor-substrate competition for the TonB homolog FusB suggests a model for ferredoxin import.The Journal of biological chemistry · 2026Article
- Acquired resistance in Stenotrophomonas maltophilia: Mechanisms underlying the shift from multidrug to pandrug resistance.European journal of microbiology & immunology · 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
- Revealing Microbial Siderophores: From Genes to Applications.Microorganisms · 2026Review
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Evolution of rhizobial siderophore utilization via accessory xeno-siderophore receptors and flexible intake machinery for self-produced siderophores.The ISME journal · 2026Article
- Ferrichrome: bacterial function, synthetic mimics, and biomedical applications.Frontiers in microbiology · 2026Review
- Molecular evolution and adaptations ofFrontiers in cellular and infection microbiology · 2026Review
- Inhibiting heme piracy by pathogenic Escherichia coli using de novo-designed proteins.Nature communications · 2025Article
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- Antibacterial microcins are ubiquitous and functionally diverse across bacterial communities.Nature communications · 2025Article
- Telomere bacteriophages are widespread and equip their bacterial hosts with potent interbacterial weapons.Science advances · 2025Article
- Lacritin cleavage-potentiated targeting of iron - respiratory reciprocity promotes bacterial death.The Journal of biological chemistry · 2025Article
- Targeting Siderophore Biosynthesis to Thwart Microbial Growth.International journal of molecular sciences · 2025Review
- 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
- A putative glucose-1-phosphate thymidylyltransferase is required for virulence, membrane-associated mechanisms, and tolerance to external stresses inFrontiers in plant science · 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
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer membranes (OM) of Gram-negative bacteria contain a class of proteins (TBDTs) that require energy for the import of nutrients and to serve as receptors for phages and protein toxins. Energy is derived from the proton motif force (pmf) of the cytoplasmic membrane (CM) through the action of three proteins, namely, TonB, ExbB, and ExbD, which are located in the CM and extend into the periplasm. The leaky phenotype of exbB exbD mutants is caused by partial complementation by homologous tolQ tolR. TonB, ExbB, and ExbD are genuine components of an energy transmission system from the CM into the OM. Mutant analyses, cross-linking experiments, and most recently X-ray and cryo-EM determinations were undertaken to arrive at a model that describes the energy transfer from the CM into the OM. These results are discussed in this paper. ExbB forms a pentamer with a pore inside, in which an ExbD dimer resides. This complex harvests the energy of the pmf and transmits it to TonB. TonB interacts with the TBDT at the TonB box, which triggers a conformational change in the TBDT that releases bound nutrients and opens the pore, through which nutrients pass into the periplasm. The structurally altered TBDT also changes the interactions of its periplasmic signaling domain with anti-sigma factors, with the consequence being that the sigma factors initiate transcription.
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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.