ArticleNature2013
Structural basis for the drug extrusion mechanism by a MATE multidrug transporter.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 117 papers.
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Who cites it
117 citing papers in PubMed, 257 citations in OpenAlex.
- Benchmarking AI Protein Structure Predictors Reveals a Persistent Bias in Multi-State Proteins.bioRxiv : the preprint server for biology · 2026Article
- StrEAMM-Thioether: Efficient Structure Prediction for Thioether-Linked Cyclic Peptides.The journal of physical chemistry. B · 2026Article
- Stapled histone H3 tails are super-substrates for lysine methyltransferase SETD7.Chemical science · 2026Article
- Expression and Purification of a Multidrug Transporter PfMATE for Structural Analyses Using Solution NMR.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Proposed mechanism for Rft1-mediated scrambling of a dolichol-linked oligosaccharide.bioRxiv : the preprint server for biology · 2025Article
- Calculation of minimum energy pathways in transport proteins.Communications chemistry · 2025Article
- The MATE family transporter CaDTX12 confers cadmium accumulation in pepper (Capsicum annuum L.).Functional & integrative genomics · 2025Article
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Structural insights into a citrate transporter that mediates aluminum tolerance in barley.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure of a lasso peptide bound ETNature communications · 2025Article
- Antibacterial macrocyclic peptides reveal a distinct mode of BamA inhibition.Nature communications · 2025Article
- The Role of Protonation in the PfMATE Transporter Protein Structural Transitions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Characterization of AlPlanta · 2024Article
- Identification and characterisation of two functional antibiotic MATE efflux pumps in the archaeon Halorubrum amylolyticum.npj antimicrobials and resistance · 2024Article
- Efflux pumps: gatekeepers of antibiotic resistance inMicrobial cell (Graz, Austria) · 2024Article
- Antibiotic Potentiation Through Phytochemical-Based Efflux Pump Inhibitors to Combat Multidrug Resistance Bacteria.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2024Review
- Metal nanoparticles as inhibitors of enzymes and toxins of multidrug-resistantInfectious medicine · 2023Review
- Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of ZnNature communications · 2023Article
- Conformational analysis and interaction of theFrontiers in chemistry · 2023Article
- The culmination of multidrug-resistant efflux pumps vs. meager antibiotic arsenal era: Urgent need for an improved new generation of EPIs.Frontiers in microbiology · 2023Review
57 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug and toxic compound extrusion (MATE) family transporters are conserved in the three primary domains of life (Archaea, Bacteria and Eukarya), and export xenobiotics using an electrochemical gradient of H(+) or Na(+) across the membrane. MATE transporters confer multidrug resistance to bacterial pathogens and cancer cells, thus causing critical reductions in the therapeutic efficacies of antibiotics and anti-cancer drugs, respectively. Therefore, the development of MATE inhibitors has long been awaited in the field of clinical medicine. Here we present the crystal structures of the H(+)-driven MATE transporter from Pyrococcus furiosus in two distinct apo-form conformations, and in complexes with a derivative of the antibacterial drug norfloxacin and three in vitro selected thioether-macrocyclic peptides, at 2.1-3.0 Å resolutions. The structures, combined with functional analyses, show that the protonation of Asp 41 on the amino (N)-terminal lobe induces the bending of TM1, which in turn collapses the N-lobe cavity, thereby extruding the substrate drug to the extracellular space. Moreover, the macrocyclic peptides bind the central cleft in distinct manners, which correlate with their inhibitory activities. The strongest inhibitory peptide that occupies the N-lobe cavity may pave the way towards the development of efficient inhibitors against MATE 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.