ArticleNature chemical biology2014
Protonation drives the conformational switch in the multidrug transporter LmrP.
Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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Who cites it
46 citing papers in PubMed, 74 citations in OpenAlex.
- Modeling protein conformational ensembles by guiding AlphaFold2 with Double Electron Electron Resonance (DEER) distance distributions.Nature communications · 2025Article
- Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and β-lactam antibiotic resistance.Nature communications · 2024Article
- 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
- Inhibition of Multidrug Efflux Pumps Belonging to the Major Facilitator Superfamily in Bacterial Pathogens.Biomedicines · 2023Review
- The Major Facilitator Superfamily and Antimicrobial Resistance Efflux Pumps of the ESKAPEE PathogenAntibiotics (Basel, Switzerland) · 2023Review
- Sampling alternative conformational states of transporters and receptors with AlphaFold2.eLife · 2022Article
- Protein functional dynamics from the rigorous global analysis of DEER data: Conditions, components, and conformations.The Journal of general physiology · 2021Article
- Molecular mechanism of sugar transport in plants unveiled by structures of glucose/HNature plants · 2021Article
- AlphaFold2 predicts the inward-facing conformation of the multidrug transporter LmrP.Proteins · 2021Article
- Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins.International journal of molecular sciences · 2021Review
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter.Nature communications · 2020Article
- Complexities of a protonatable substrate in measurements of Hoechst 33342 transport by multidrug transporter LmrP.Scientific reports · 2020Article
- The Multidrug Transporter MdfA Deviates from the Canonical Model of Alternating Access of MFS Transporters.Journal of molecular biology · 2020Article
- An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity.Nature structural & molecular biology · 2020Article
- Site-specific resolution of anionic residues in proteins using solid-state NMR spectroscopy.Journal of biomolecular NMR · 2020Article
- Sequence and structural determinants of ligand-dependent alternating access of a MATE transporter.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily.Scientific reports · 2020Article
- Functional and Structural Roles of the Major Facilitator Superfamily Bacterial Multidrug Efflux Pumps.Microorganisms · 2020Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Multidrug antiporters of the major facilitator superfamily couple proton translocation to the extrusion of cytotoxic molecules. The conformational changes that underlie the transport cycle and the structural basis of coupling of these transporters have not been elucidated. Here we used extensive double electron-electron resonance measurements to uncover the conformational equilibrium of LmrP, a multidrug transporter from Lactococcus lactis, and to investigate how protons and ligands shift this equilibrium to enable transport. We find that the transporter switches between outward-open and outward-closed conformations, depending on the protonation states of specific acidic residues forming a transmembrane protonation relay. Our data can be framed in a model of transport wherein substrate binding initiates the transport cycle by opening the extracellular side. Subsequent protonation of membrane-embedded acidic residues induces substrate release to the extracellular side and triggers a cascade of conformational changes that concludes in proton release to the intracellular side.
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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.