Scientific article
Open access

The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells

Published inScience advances, vol. 8, no. 41, p. 1-14; eabn6845
Publication date2022-10-14

Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to truly understand the biophysical properties of membrane proteins in a physiological environment, they must be investigated within living cells. Here, we used a spin-labeled nanobody to interrogate the conformational cycle of the ABC transporter MsbA by double electron-electron resonance. Unexpectedly, the wide inward-open conformation of MsbA, commonly considered a nonphysiological state, was found to be prominently populated in Escherichia coli cells. Molecular dynamics simulations revealed that extensive lateral portal opening is essential to provide access of its large natural substrate core lipid A to the binding cavity. Our work paves the way to investigate the conformational landscape of membrane proteins in cells.

Affiliation Not a UNIGE publication
Citation (ISO format)
GALAZZO, Laura et al. The ABC transporter MsbA adopts the wide inward-open conformation in <i>E. coli</i> cells. In: Science advances, 2022, vol. 8, n° 41, p. 1–14. doi: 10.1126/sciadv.abn6845
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Article (Published version)
ISSN of the journal2375-2548

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