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Structural insight into the role of the Ton complex in energy transduction

Author

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  • Hervé Celia

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, UMR7255 CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée
    National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health)

  • Nicholas Noinaj

    (Markey Center for Structural Biology, and the Purdue Institute for Inflammation, Immunology and Infectious Diseases, Purdue University)

  • Stanislav D. Zakharov

    (Markey Center for Structural Biology, and the Purdue Institute for Inflammation, Immunology and Infectious Diseases, Purdue University)

  • Enrica Bordignon

    (Fachbereich Physik, Freie Universität
    Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum)

  • Istvan Botos

    (National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health)

  • Monica Santamaria

    (Instituto de Investigacion Hospital La Paz (IdiPAZ), Paseo de la Castellana 261)

  • Travis J. Barnard

    (National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health)

  • William A. Cramer

    (Markey Center for Structural Biology, and the Purdue Institute for Inflammation, Immunology and Infectious Diseases, Purdue University)

  • Roland Lloubes

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires, UMR7255 CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée)

  • Susan K. Buchanan

    (National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health)

Abstract

In Gram-negative bacteria, outer membrane transporters import nutrients by coupling to an inner membrane protein complex called the Ton complex. The Ton complex consists of TonB, ExbB, and ExbD, and uses the proton motive force at the inner membrane to transduce energy to the outer membrane via TonB. Here, we structurally characterize the Ton complex from Escherichia coli using X-ray crystallography, electron microscopy, double electron–electron resonance (DEER) spectroscopy, and crosslinking. Our results reveal a stoichiometry consisting of a pentamer of ExbB, a dimer of ExbD, and at least one TonB. Electrophysiology studies show that the Ton subcomplex forms pH-sensitive cation-selective channels and provide insight into the mechanism by which it may harness the proton motive force to produce energy.

Suggested Citation

  • Hervé Celia & Nicholas Noinaj & Stanislav D. Zakharov & Enrica Bordignon & Istvan Botos & Monica Santamaria & Travis J. Barnard & William A. Cramer & Roland Lloubes & Susan K. Buchanan, 2016. "Structural insight into the role of the Ton complex in energy transduction," Nature, Nature, vol. 538(7623), pages 60-65, October.
    • Handle: RePEc:nat:nature:v:538:y:2016:i:7623:d:10.1038_nature19757
    DOI: 10.1038/nature19757
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    Cited by:

    1. Maximilian Zinke & Maylis Lejeune & Ariel Mechaly & Benjamin Bardiaux & Ivo Gomperts Boneca & Philippe Delepelaire & Nadia Izadi-Pruneyre, 2024. "Ton motor conformational switch and peptidoglycan role in bacterial nutrient uptake," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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