The ABC transporter MsbA adopts the wide inward-open conformation in
Journal
Science advances
ISSN: 2375-2548
Titre abrégé: Sci Adv
Pays: United States
ID NLM: 101653440
Informations de publication
Date de publication:
14 10 2022
14 10 2022
Historique:
entrez:
12
10
2022
pubmed:
13
10
2022
medline:
15
10
2022
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 36223470
doi: 10.1126/sciadv.abn6845
pmc: PMC9555771
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Bacterial Proteins
0
Detergents
0
Escherichia coli Proteins
0
Lipid A
0
Liposomes
0
Membrane Proteins
0
MsbA protein, Bacteria
0
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
eabn6845Références
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