ArticleThe Journal of biological chemistry2016
Identification of the High-affinity Substrate-binding Site of the Multidrug and Toxic Compound Extrusion (MATE) Family Transporter from Pseudomonas stutzeri.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Membrane Efflux Pumps of PathogenicMicroorganisms · 2022Review
- The structure of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters.Journal of molecular biology · 2021Review
- Engineered MATE multidrug transporters reveal two functionally distinct ion-coupling pathways in NorM from Vibrio cholerae.Communications biology · 2021Article
- 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
- Antibiotic ResistantFoods (Basel, Switzerland) · 2019Review
- 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
- Structural basis for xenobiotic extrusion by eukaryotic MATE transporter.Nature communications · 2017Article
- Conserved binding site in the N-lobe of prokaryotic MATE transporters suggests a role for NaThe Journal of biological chemistryArticle
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug and toxic compound extrusion (MATE) transporters exist in all three domains of life. They confer multidrug resistance by utilizing H(+) or Na(+) electrochemical gradients to extrude various drugs across the cell membranes. The substrate binding and the transport mechanism of MATE transporters is a fundamental process but so far not fully understood. Here we report a detailed substrate binding study of NorM_PS, a representative MATE transporter from Pseudomonas stutzeri Our results indicate that NorM_PS is a proton-dependent multidrug efflux transporter. Detailed binding studies between NorM_PS and 4',6-diamidino-2-phenylindole (DAPI) were performed by isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), and spectrofluorometry. Two exothermic binding events were observed from ITC data, and the high-affinity event was directly correlated with the extrusion of DAPI. The affinities are about 1 μm and 0.1 mm for the high and low affinity binding, respectively. Based on our homology model of NorM_PS, variants with mutations of amino acids that are potentially involved in substrate binding, were constructed. By carrying out the functional characterization of these variants, the critical amino acid residues (Glu-257 and Asp-373) for high-affinity DAPI binding were determined. Taken together, our results suggest a new substrate-binding site for MATE transporters.
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