ArticleThe Journal of biological chemistry2010
Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 61 citations in OpenAlex.
- Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.bioRxiv : the preprint server for biology · 2026Article
- 18-Crown-6-ether Utilizes Distinct Allosteric Interactions to Uncouple Transport by the Multidrug Efflux Pump EmrE.Biochemistry · 2025Article
- The C-terminus of the multi-drug efflux pump EmrE prevents proton leak by gating transport.eLife · 2025Article
- 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
- Article
- High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport.Nature communications · 2022Article
- Molecular mechanism of proton-coupled ligand translocation by the bacterial efflux pump EmrE.PLoS computational biology · 2021Article
- Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021Review
- 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
- The structural basis of promiscuity in small multidrug resistance transporters.Nature communications · 2020Article
- ATP-dependent interactions of a cargo protein with the transmembrane domain of a polypeptide processing and secretion ABC transporter.The Journal of biological chemistry · 2020Article
- Identification of an Alternating-Access Dynamics Mutant of EmrE with Impaired Transport.Journal of molecular biology · 2019Article
- The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release.The Journal of biological chemistry · 2018Article
- Few Conserved Amino Acids in the Small Multidrug Resistance Transporter EmrE Influence Drug Polyselectivity.Antimicrobial agents and chemotherapy · 2018Article
- Article
- New free-exchange model of EmrE transport.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE.Nature chemical biology · 2016Article
- Protonation-dependent conformational dynamics of the multidrug transporter EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
EmrE, a member of the small multidrug transporters superfamily, extrudes positively charged hydrophobic compounds out of Escherichia coli cytoplasm in exchange for inward movement of protons down their electrochemical gradient. Although its transport mechanism has been thoroughly characterized, the structural basis of energy coupling and the conformational cycle mediating transport have yet to be elucidated. In this study, EmrE structure in liposomes and the substrate-induced conformational changes were investigated by systematic spin labeling and EPR analysis. Spin label mobilities and accessibilities describe a highly dynamic ligand-free (apo) conformation. Dipolar coupling between spin labels across the dimer reveals at least two spin label populations arising from different packing interfaces of the EmrE dimer. One population is consistent with antiparallel arrangement of the monomers, although the EPR parameters suggest deviations from the crystal structure of substrate-bound EmrE. Resolving these discrepancies requires an unusual disposition of TM3 relative to the membrane-water interface and a kink in its backbone that enables bending of its C-terminal part. Binding of the substrate tetraphenylphosphonium changes the environment of spin labels and their proximity in three transmembrane helices. The underlying conformational transition involves repacking of TM1, tilting of TM2, and changes in the backbone configurations of TM3 and the adjacent loop connecting it to TM4. A dynamic apo conformation is necessary for the polyspecificity of EmrE allowing the binding of structurally diverse substrates. The flexibility of TM3 may play a critical role in movement of substrates across the membrane.
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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.