ArticleThe Journal of biological chemistry2014
Multidrug transport protein norM from vibrio cholerae simultaneously couples to sodium- and proton-motive force.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Structural basis of drug recognition by human MATE1 transporter.Nature communications · 2025Article
- Exploring the Structural Dynamics of LeuT Using EPR Spectroscopy: A Focus on Transmembrane Helix 10.Journal of neurochemistry · 2025Article
- The Role of Protonation in the PfMATE Transporter Protein Structural Transitions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022Review
- The Bacterial Cell Wall: From Lipid II Flipping to Polymerization.Chemical reviews · 2022Review
- Membrane Efflux Pumps of PathogenicMicroorganisms · 2022Review
- Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters.Journal of molecular biology · 2021Review
- The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.Chemical reviews · 2021Article
- Engineered MATE multidrug transporters reveal two functionally distinct ion-coupling pathways in NorM from Vibrio cholerae.Communications biology · 2021Article
- The Structure and Mechanism of Drug Transporters.Methods in molecular biology (Clifton, N.J.) · 2021Article
- NamBio · 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
- A Novel MFS-MDR Transporter, MdrP, Employs D223 as a Key Determinant in the NaFrontiers in microbiology · 2020Article
- Inward-facing conformation of a multidrug resistance MATE family transporter.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural Basis of HStructure (London, England : 1993) · 2019Article
- Multidrug efflux pumps: structure, function and regulation.Nature reviews. Microbiology · 2018Review
- Broadly conserved NaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Sodium and proton coupling in the conformational cycle of a MATE antiporter fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Direct observation of the influence of cardiolipin and antibiotics on lipid II binding to MurJ.Nature chemistry · 2018Article
- Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.The Journal of membrane biology · 2018Article
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3 authors.
Funding
Abstract
Membrane transporters belonging to the multidrug and toxic compound extrusion family mediate the efflux of unrelated pharmaceuticals from the interior of the cell in organisms ranging from bacteria to human. These proteins are thought to fall into two classes that couple substrate efflux to the influx of either Na(+) or H(+). We studied the energetics of drug extrusion by NorM from Vibrio cholerae in proteoliposomes in which purified NorM protein was functionally reconstituted in an inside-out orientation. We establish that NorM simultaneously couples to the sodium-motive force and proton-motive force, and biochemically identify protein regions and residues that play important roles in Na(+) or H(+) binding. As the positions of protons are not available in current medium and high-resolution crystal structures of multidrug and toxic compound extrusion transporters, our findings add a previously unrecognized parameter to mechanistic models based of these structures.
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