ArticleProceedings of the National Academy of Sciences of the United States of America2022
HDX-MS performed on BtuB in
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Probing protein-lipid interactions by hydrogen/deuterium exchange-mass spectrometry: advances, challenges and future directions.Chemical science · 2026Review
- Structural dynamics and immunogenicity of the recombinant and outer membrane vesicle-embedded Meningococcal antigen NadA.Nature communications · 2026Article
- Article
- Allosteric effects of the coupling cation in melibiose transporter MelB.bioRxiv : the preprint server for biology · 2025Article
- Practical Tips for the Application of HDX-MS to Membrane Proteins, Biomolecular Condensates, and Weak Protein Binders.Journal of the American Society for Mass Spectrometry · 2025Article
- Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- An adaptive biomolecular condensation response is conserved across environmentally divergent species.Nature communications · 2024Article
- HDX-MS finds that partial unfolding with sequential domain activation controls condensation of a cellular stress marker.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mobile barrier mechanisms for NaeLife · 2024Article
- Hydrophilic Interaction Liquid Chromatography at Subzero Temperature for Hydrogen-Deuterium Exchange Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.eLife · 2023Article
- Mobile barrier mechanisms for NabioRxiv : the preprint server for biology · 2023Article
- An adaptive biomolecular condensation response is conserved across environmentally divergent species.bioRxiv : the preprint server for biology · 2023Article
- Article
- Hydrogen/deuterium exchange-mass spectrometry of integral membrane proteins in native-like environments: current scenario and the way forward.Essays in biochemistry · 2023Article
- Structural mass spectrometry approaches to understand multidrug efflux systems.Essays in biochemistry · 2023Review
- GdJournal of the American Chemical Society · 2023Article
- Development of in vivo HDX-MS with applications to a TonB-dependent transporter and other proteins.Protein science : a publication of the Protein Society · 2022Article
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4 authors.
Funding
Abstract
To import large metabolites across the outer membrane of gram-negative bacteria, TonB-dependent transporters (TBDTs) undergo significant conformational change. After substrate binding in BtuB, the Escherichia coli vitamin B12 TBDT, TonB binds and couples BtuB to the inner-membrane proton motive force that powers transport [N. Noinaj, M. Guillier, T. J. Barnard, S. K. Buchanan, Annu. Rev. Microbiol. 64, 43–60 (2010)]. However, the role of TonB in rearranging the plug domain of BtuB to form a putative pore remains enigmatic. Some studies focus on force-mediated unfolding [S. J. Hickman, R. E. M. Cooper, L. Bellucci, E. Paci, D. J. Brockwell, Nat. Commun. 8, 14804 (2017)], while others propose force-independent pore formation by TonB binding [T. D. Nilaweera, D. A. Nyenhuis, D. S. Cafiso, eLife 10, e68548 (2021)], leading to breakage of a salt bridge termed the “Ionic Lock.” Our hydrogen–deuterium exchange/mass spectrometry (HDX-MS) measurements in E. coli outer membranes find that the region surrounding the Ionic Lock, far from the B12 site, is fully destabilized upon substrate binding. A comparison of the exchange between the B12-bound and the B12+TonB–bound complexes indicates that B12 binding is sufficient to unfold the Ionic Lock region, with the subsequent binding of a TonB fragment having much weaker effects. TonB binding accelerates exchange in the third substrate-binding loop, but pore formation does not obviously occur in this or any region. This study provides a detailed structural and energetic description of the early stages of B12 passage that provides support both for and against current models of the transport process.
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