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Expulsion mechanism of the substrate-translocating subunit in ECF transporters

Author

Listed:
  • Chancievan Thangaratnarajah

    (University of Groningen
    University of Groningen)

  • Mark Nijland

    (University of Groningen)

  • Luís Borges-Araújo

    (CNRS and University of Lyon)

  • Aike Jeucken

    (University of Groningen)

  • Jan Rheinberger

    (University of Groningen
    University of Groningen
    University of Heidelberg)

  • Siewert J. Marrink

    (University of Groningen)

  • Paulo C. T. Souza

    (CNRS and University of Lyon)

  • Cristina Paulino

    (University of Groningen
    University of Groningen
    University of Heidelberg)

  • Dirk J. Slotboom

    (University of Groningen)

Abstract

Energy-coupling factor (ECF)-type transporters mediate the uptake of micronutrients in many bacteria. They consist of a substrate-translocating subunit (S-component) and an ATP-hydrolysing motor (ECF module) Previous data indicate that the S-component topples within the membrane to alternately expose the binding site to either side of the membrane. In many ECF transporters, the substrate-free S-component can be expelled from the ECF module. Here we study this enigmatic expulsion step by cryogenic electron microscopy and reveal that ATP induces a concave-to-convex shape change of two long helices in the motor, thereby destroying the S-component’s docking site and allowing for its dissociation. We show that adaptation of the membrane morphology to the conformational state of the motor may favour expulsion of the substrate-free S-component when ATP is bound and docking of the substrate-loaded S-component after hydrolysis. Our work provides a picture of bilayer-assisted chemo-mechanical coupling in the transport cycle of ECF transporters.

Suggested Citation

  • Chancievan Thangaratnarajah & Mark Nijland & Luís Borges-Araújo & Aike Jeucken & Jan Rheinberger & Siewert J. Marrink & Paulo C. T. Souza & Cristina Paulino & Dirk J. Slotboom, 2023. "Expulsion mechanism of the substrate-translocating subunit in ECF transporters," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40266-1
    DOI: 10.1038/s41467-023-40266-1
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    References listed on IDEAS

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