Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from Bacillus subtilis - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Communications Biology Année : 2019

Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from Bacillus subtilis

Résumé

ATP-binding-cassette (ABC) transporters are molecular pumps that translocate molecules across the cell membrane by switching between inward-facing and outward-facing states. To obtain a detailed understanding of their mechanism remains a challenge to structural biology, as these proteins are notoriously difficult to study at the molecular level in their active, membrane-inserted form. Here we use solid-state NMR to investigate the multidrug ABC transporter BmrA reconstituted in lipids. We identify the chemical-shift differences between the inward-facing, and outward-facing state induced by ATP:Mg 2+ :Vi addition. Analysis of an X-loop mutant, for which we show that ATPase and transport activities are uncoupled, reveals an incomplete transition to the outward-facing state upon ATP:Mg 2+ :Vi addition, notably lacking the decrease in dynamics of a defined set of residues observed in wild-type BmrA. This suggests that this stiffening is required for an efficient transmission of the conformational changes to allow proper transport of substrate by the pump.
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Dates et versions

hal-02322611 , version 1 (21-10-2019)

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Denis Lacabanne, Cédric Orelle, Lauriane Lecoq, Britta Kunert, Claire Chuilon, et al.. Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from Bacillus subtilis. Communications Biology, 2019, 2 (1), ⟨10.1038/s42003-019-0390-x⟩. ⟨hal-02322611⟩
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