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Cryo-EM structures of the E. coli Ton and Tol motor complexes

Author

Listed:
  • Herve Celia

    (National Institutes of Health)

  • Istvan Botos

    (National Institutes of Health)

  • Rodolfo Ghirlando

    (National Institutes of Health)

  • Denis Duché

    (Institut de Microbiologie de la Méditerranée)

  • Bridgette M. Beach

    (National Institutes of Health)

  • Roland Lloubes

    (Institut de Microbiologie de la Méditerranée)

  • Susan K. Buchanan

    (National Institutes of Health)

Abstract

The Ton and Tol motor proteins use the proton gradient at the inner membrane of Gram-negative bacteria as an energy source. The generated force is transmitted through the periplasmic space to protein components associated with the outer membrane, either to maintain the outer membrane integrity for the Tol system, or to allow essential nutrients to enter the cell for Ton. We have solved the high-resolution structures of the E. coli TonB-ExbB-ExbD and TolA-TolQ-TolR complexes, revealing the inner membrane embedded engine parts of the Ton and Tol systems, and showing how TonB and TolA interact with the ExbBD and TolQR subcomplexes. Structural similarities between the two motor complexes suggest a common mechanism for the opening of the proton channel and the propagation of the proton motive force into movement of the TonB and TolA subunits. Because TonB and TolA bind at preferential ExbB or TolQ subunits, we propose a new mechanism of assembly of TonB and TolA with their respective ExbBD and TolQR subcomplexes and discuss its impact on the mechanism of action for the Ton and Tol systems.

Suggested Citation

  • Herve Celia & Istvan Botos & Rodolfo Ghirlando & Denis Duché & Bridgette M. Beach & Roland Lloubes & Susan K. Buchanan, 2025. "Cryo-EM structures of the E. coli Ton and Tol motor complexes," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-61286-z
    DOI: 10.1038/s41467-025-61286-z
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    References listed on IDEAS

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    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.
    2. Haidai Hu & Philipp F. Popp & Mònica Santiveri & Aritz Roa-Eguiara & Yumeng Yan & Freddie J. O. Martin & Zheyi Liu & Navish Wadhwa & Yong Wang & Marc Erhardt & Nicholas M. I. Taylor, 2023. "Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. 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.
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    1. Wee Boon Tan & Shu-Sin Chng, 2025. "Primary role of the Tol-Pal complex in bacterial outer membrane lipid homeostasis," Nature Communications, Nature, vol. 16(1), pages 1-11, December.
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