Expulsion mechanism of the substrate-translocating subunit in ECF transporters

Chancievan Thangaratnarajah, Mark Nijland, Luís Borges-Araújo, Aike Jeucken, Jan Rheinberger, Siewert J. Marrink, Paulo C. T. Souza, Cristina Paulino () and Dirk J. Slotboom ()
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Chancievan Thangaratnarajah: 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
Siewert J. Marrink: University of Groningen
Paulo C. T. Souza: CNRS and University of Lyon
Cristina Paulino: University of Groningen
Dirk J. Slotboom: University of Groningen

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-40266-1

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