ArticleThe Journal of biological chemistry2009
The secondary multidrug/proton antiporter MdfA tolerates displacements of an essential negatively charged side chain.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Molecular Dynamics Simulation Analyses of the Conformational Change of an Escherichia coli Multidrug Exporter, MdfA.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular determinants of substrate specificity in the efflux pump CraA fromMicrobiology spectrum · 2025Article
- Review
- Proton-driven alternating access in a spinster lipid transporter.Nature communications · 2022Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- The Multidrug Transporter MdfA Deviates from the Canonical Model of Alternating Access of MFS Transporters.Journal of molecular biology · 2020Article
- Dynamical Behavior of the Human Ferroportin Homologue fromInternational journal of molecular sciences · 2020Article
- Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily.Scientific reports · 2020Article
- Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels.Scientific reports · 2019Article
- smFRET Probing Reveals Substrate-Dependent Conformational Dynamics of E. coli Multidrug MdfA.Biophysical journal · 2019Article
- Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition.Communications biology · 2019Article
- Outward open conformation of a Major Facilitator Superfamily multidrug/HNature communications · 2018Article
- The ins and outs of vesicular monoamine transporters.The Journal of general physiology · 2018Review
- Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.The Journal of membrane biology · 2018Article
- Proton-solute coupling mechanism of the maltose transporter from Saccharomyces cerevisiae.Scientific reports · 2017Article
- Energy coupling mechanisms of MFS transporters.Protein science : a publication of the Protein Society · 2015Review
- Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.Cell research · 2015Article
- Escherichia coli YqjA, a Member of the Conserved DedA/Tvp38 Membrane Protein Family, Is a Putative Osmosensing Transporter Required for Growth at Alkaline pH.Journal of bacteriology · 2015Article
- Functionally important carboxyls in a bacterial homologue of the vesicular monoamine transporter (VMAT).The Journal of biological chemistry · 2014Article
- Members of the conserved DedA family are likely membrane transporters and are required for drug resistance in Escherichia coli.Antimicrobial agents and chemotherapy · 2014Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The largest family of solute transporters includes ion motive force-driven secondary transporters. Several well characterized solute-specific transport systems in this group have at least one irreplaceable acidic residue that plays a critical role in energy coupling during transport. Previous studies have established the importance of acidic residues in substrate recognition by major facilitator superfamily secondary multidrug transporters, but their role in the transport mechanism remained unknown. We have been investigating the involvement of acidic residues in the mechanism of MdfA, an Escherichia coli secondary multidrug/proton antiporter. We demonstrated that no single negatively charged side chain plays an irreplaceable role in MdfA. Accordingly, we hypothesized that MdfA might be able to utilize at least two acidic residues alternatively. In this study, we present evidence that indeed, unlike solute-specific secondary transporters, MdfA tolerates displacements of an essential negative charge to various locations in the putative drug translocation pathway. The results suggest that MdfA utilizes a proton translocation strategy that is less sensitive to perturbations in the geometry of the proton-binding site, further illustrating the exceptional structural promiscuity of multidrug transporters.
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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.