ArticleNature communications2021
Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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Who cites it
55 citing papers in PubMed, 105 citations in OpenAlex.
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- Cryo-EM structures of Cdr1 reveal snapshots of substrate transport and diverse inhibitor recognition.Science advances · 2026Article
- Membrane Access and Orbital Localization Govern ABC Transporter Substrate Recognition.Molecules (Basel, Switzerland) · 2026Article
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- Structural basis of lipid-linked galactan export by the mycobacterial ABC transporter Wzm-Wzt.Nature communications · 2026Article
- Pamamycin Disrupts the Cell Envelope and Mitochondrial Potential to InhibitFoods (Basel, Switzerland) · 2026Article
- MFS-transporter Flr1 is a major drug-efflux transporter in Saccharomyces cerevisiae ascospores.FEMS yeast research · 2026Article
- The Velvet protein vea: a key positive regulator of growth and cordycepin biosynthesis in Cordyceps militaris.Microbial cell factories · 2025Article
- Transcriptomic studies on the product stress response revealed that YCF1 is a beneficial factor for progesterone production inSynthetic and systems biotechnology · 2025Article
- Multidrug efflux pumps and innate azole resistance of Mucor lusitanicus.The Journal of antimicrobial chemotherapy · 2025Article
- A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural Basis for Oxidized Glutathione Recognition by Yeast Cadmium Factor 1.Journal of the American Chemical Society · 2025Article
- Enhanced vitamin A production by engineering transporters, ATP and precursor supply.Biodesign research · 2025Article
- A key residue of the extracellular gate provides quality control contributing to ABCG substrate specificity.Nature communications · 2025Article
- Message hidden in α-helices-toward a better understanding of plant ABCG transporters' multispecificity.Plant physiology · 2025Article
- Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Pdr5, a member of the extensive ABC transporter superfamily, is representative of a clinically relevant subgroup involved in pleiotropic drug resistance. Pdr5 and its homologues drive drug efflux through uncoupled hydrolysis of nucleotides, enabling organisms such as baker's yeast and pathogenic fungi to survive in the presence of chemically diverse antifungal agents. Here, we present the molecular structure of Pdr5 solved with single particle cryo-EM, revealing details of an ATP-driven conformational cycle, which mechanically drives drug translocation through an amphipathic channel, and a clamping switch within a conserved linker loop that acts as a nucleotide sensor. One half of the transporter remains nearly invariant throughout the cycle, while its partner undergoes changes that are transmitted across inter-domain interfaces to support a peristaltic motion of the pumped molecule. The efflux model proposed here rationalises the pleiotropic impact of Pdr5 and opens new avenues for the development of effective antifungal compounds.
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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.