Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
10 05 2023
10 05 2023
Historique:
medline:
11
5
2023
pubmed:
25
4
2023
entrez:
25
4
2023
Statut:
ppublish
Résumé
The bacterial transporter EmrE is a homo-dimeric membrane protein that effluxes cationic polyaromatic substrates against the concentration gradient by coupling to proton transport. As the archetype of the small multidrug resistance family of transporters, EmrE structure and dynamics provide atomic insights into the mechanism of transport by this family of proteins. We recently determined high-resolution structures of EmrE in complex with a cationic substrate, tetra(4-fluorophenyl)phosphonium (F
Identifiants
pubmed: 37097985
doi: 10.1021/jacs.3c00340
doi:
Substances chimiques
Escherichia coli Proteins
0
Lipid Bilayers
0
Protons
0
Antiporters
0
Membrane Transport Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
10104-10115Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM141748
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM111135
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM132079
Pays : United States