ArticleBiochemistry2013
Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Receptor-substrate competition for the TonB homolog FusB suggests a model for ferredoxin import.The Journal of biological chemistry · 2026Article
- Comprehensive genomic analysis of type VI secretion system diversity and associated proteins inMicrobial genomics · 2025Article
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Experimental and computational methods to highlight behavioural variations in TonB-dependent transporter expression in Pseudomonas aeruginosa versus siderophore concentration.Scientific reports · 2023Article
- Surveying membrane landscapes: a new look at the bacterial cell surface.Nature reviews. Microbiology · 2023Review
- A disulfide chaperone knockout facilitates spin labeling and pulse EPR spectroscopy of outer membrane transporters.Protein science : a publication of the Protein Society · 2023Article
- HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Ton Motor.Frontiers in microbiology · 2022Review
- Structural intermediates observed only in intacteLife · 2021Article
- Extracellular loops of BtuB facilitate transport of vitamin B12 through the outer membrane of E. coli.PLoS computational biology · 2020Article
- Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020Review
- Inhibiting the copper efflux system in microbes as a novel approach for developing antibiotics.PloS one · 2019Article
- Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein.PloS one · 2019Article
- Evolution and Sequence Diversity of FhuA in Salmonella and Escherichia.Infection and immunity · 2018Article
- Article
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Article
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.Protein science : a publication of the Protein Society · 2017Article
- EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.Biophysical journal · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The energy-dependent uptake of trace nutrients by Gram-negative bacteria involves the coupling of an outer membrane transport protein to the transperiplasmic protein TonB. In this study, a soluble construct of Escherichia coli TonB (residues 33-239) was used to determine the affinity of TonB for outer membrane transporters BtuB, FecA, and FhuA. Using fluorescence anisotropy, TonB(33-239) was found to bind with high affinity (tens of nanomolar) to both BtuB and FhuA; however, no high-affinity binding to FecA was observed. In BtuB, the high-affinity binding of TonB(33-239) was eliminated by mutations in the Ton box, which yield transport-defective protein, or by the addition of a Colicin E3 fragment, which stabilizes the Ton box in a folded state. These results indicate that transport requires a high-affinity transporter-TonB interaction that is mediated by the Ton box. Characterization of TonB(33-239) using double electron-electron resonance (DEER) demonstrates that a significant population of TonB(33-239) exists as a dimer; moreover, interspin distances are in approximate agreement with interlocked dimers observed previously by crystallography for shorter TonB fragments. When the TonB(33-239) dimer is bound to the outer membrane transporter, DEER shows that the TonB(33-239) dimer is converted to a monomeric form, suggesting that a dimer-monomer conversion takes place at the outer membrane during the TonB-dependent transport cycle.
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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.