ArticleNature chemical biology2016
Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 73 citations in OpenAlex.
- Proton hopping and secondary gating reveal a universal transport mechanism in a minimal bacterial transporter EmrE.Biophysical journal · 2026Article
- Conduction pathway for potassium through theeLife · 2025Article
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Conduction pathway for potassium through the E. coli pump KdpFABC.bioRxiv : the preprint server for biology · 2025Article
- Quantification of Membrane Protein Conformational Free Energy from Mutations and a Single Atom.Journal of the American Chemical Society · 2025Article
- A fiducial-assisted strategy compatible with resolving small MFS transporter structures in multiple conformations using cryo-EM.Nature communications · 2025Article
- Dynamics underlie the drug recognition mechanism by the efflux transporter EmrE.Nature communications · 2024Article
- Proton-coupled transport mechanism of the efflux pump NorA.Nature communications · 2024Article
- Review
- Energy coupling and stoichiometry of ZneLife · 2023Article
- Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.Journal of the American Chemical Society · 2023Article
- Still rocking in the structural era: A molecular overview of the small multidrug resistance (SMR) transporter family.The Journal of biological chemistry · 2022Review
- Functional Role of YnfA, an Efflux Transporter in Resistance to Antimicrobial Agents in Shigella flexneri.Antimicrobial agents and chemotherapy · 2022Article
- High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport.Nature communications · 2022Article
- Asymmetric protonation of glutamate residues drives a preferred transport pathway in EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.Journal of molecular biology · 2021Review
- Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers.Nature communications · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Assembly and regulation of the chlorhexidine-specific efflux pump AceI.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.Journal of biomolecular NMR · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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 glutamate residue. These observations directly correlate with the resistance phenotype for wild-type EmrE and the E14D mutant as a function of pH. Furthermore, our results support a model in which the pH gradient across the inner membrane of E. coli may be used on a mechanistic level to shift the equilibrium of the transporter in favor of an inward-open resting conformation poised for drug binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.