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Article

Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE.

Nature chemical biology - 1 Mar 2016

Gayen Anindita, Leninger Maureen, Traaseth Nathaniel J

Abstract excerpt

Secondary active transport proteins play a central role in conferring bacterial multidrug resistance. In this work, we investigated the proton-coupled transport mechanism for the Escherichia coli drug efflux pump EmrE using NMR spectroscopy. Our results show that the global conformational motions necessary for transport are modulated in an allosteric fashion by the protonation state of a membrane-embedded...

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PMID: 26751516
DOI: 10.1038/nchembio.1999
PMCID: PMC4755857

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE.PMID 26751516Read ↗

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