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Expulsion mechanism of the substrate-translocating subunit in ECF transporters

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 expos...

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Main Authors: Thangaratnarajah, Chancievan (Author) , Nijland, Mark (Author) , Borges-Araújo, Luís (Author) , Jeucken, Aike (Author) , Rheinberger, Jan (Author) , Marrink, Siewert J. (Author) , Souza, Paulo C. T. (Author) , Batista Paulino, Cristina (Author) , Slotboom, Dirk J. (Author)
Format: Article (Journal)
Language:English
Published: 25 July 2023
In: Nature Communications
Year: 2023, Volume: 14, Pages: 1-14
ISSN:2041-1723
DOI:10.1038/s41467-023-40266-1
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41467-023-40266-1
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-023-40266-1
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Author Notes:Chancievan Thangaratnarajah, Mark Nijland, Luís Borges-Araújo, Aike Jeucken, Jan Rheinberger, Siewert J. Marrink, Paulo C.T. Souza, Cristina Paulino & Dirk J. Slotboom
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Summary: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.
Item Description:Gesehen am 31.10.2023
Physical Description:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-023-40266-1

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