ArticleeLife2019
Inducing conformational preference of the membrane protein transporter EmrE through conservative mutations.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed.
- Quantification of Membrane Protein Conformational Free Energy from Mutations and a Single Atom.Journal of the American Chemical Society · 2025Article
- Genomic and Transcriptomic Analysis of MutantFoods (Basel, Switzerland) · 2025Article
- Dynamics underlie the drug recognition mechanism by the efflux transporter EmrE.Nature communications · 2024Article
- Still rocking in the structural era: A molecular overview of the small multidrug resistance (SMR) transporter family.The Journal of biological chemistry · 2022Review
- Article
- 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
- State-selective frustration as a key driver of allosteric pluripotency.Chemical science · 2021Article
- Structural Insights into Transporter-Mediated Drug Resistance in Infectious Diseases.Journal of molecular biology · 2021Review
- Bacterial Resistance to Antimicrobial Agents.Antibiotics (Basel, Switzerland) · 2021Review
- The high-energy transition state of the glutamate transporter homologue GltPh.The EMBO journal · 2021Article
- The structural basis of promiscuity in small multidrug resistance transporters.Nature communications · 2020Article
- Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.Journal of biomolecular NMR · 2020Article
- Magnetic Alignment of Polymer Nanodiscs Probed by Solid-State NMR Spectroscopy.Langmuir : the ACS journal of surfaces and colloids · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Transporters from bacteria to humans contain inverted repeat domains thought to arise evolutionarily from the fusion of smaller membrane protein genes. Association between these domains forms the functional unit that enables transporters to adopt distinct conformations necessary for function. The small multidrug resistance (SMR) family provides an ideal system to explore the role of mutations in altering conformational preference since transporters from this family consist of antiparallel dimers that resemble the inverted repeats present in larger transporters. Here, we show using NMR spectroscopy how a single conservative mutation introduced into an SMR dimer is sufficient to change the resting conformation and function in bacteria. These results underscore the dynamic energy landscape for transporters and demonstrate how conservative mutations can influence structure and function.
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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.