The ABC transporter MsbA adopts the wide inward-open conformation in

Autor: Laura, Galazzo, Gianmarco, Meier, Dovile, Januliene, Kristian, Parey, Dario, De Vecchis, Bianca, Striednig, Hubert, Hilbi, Lars V, Schäfer, Ilya, Kuprov, Arne, Moeller, Enrica, Bordignon, Markus A, Seeger
Rok vydání: 2022
Předmět:
Zdroj: Science advances. 8(41)
ISSN: 2375-2548
Popis: 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
Databáze: OpenAIRE