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
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

10104-10115

Subventions

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

Auteurs

Alexander A Shcherbakov (AA)

Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.

Merissa Brousseau (M)

Department of Biochemistry, University of Wisconsin at Madison, Madison, Wisconsin 53706, United States.

Katherine A Henzler-Wildman (KA)

Department of Biochemistry, University of Wisconsin at Madison, Madison, Wisconsin 53706, United States.

Mei Hong (M)

Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.

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Classifications MeSH