ArticleThe Journal of biological chemistry2013
The deviant ATP-binding site of the multidrug efflux pump Pdr5 plays an active role in the transport cycle.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- Detection of PDR5-mediated alachlor efflux using a chemically induced dimer biosensor.PloS one · 2025Article
- Inhibitor-Resistant Mutants Give Important Insights into Candida albicans ABC Transporter Cdr1 Substrate Specificity and Help Elucidate Efflux Pump Inhibition.Antimicrobial agents and chemotherapy · 2022Article
- Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5.Nature communications · 2021Article
- Directed Mutational Strategies Reveal Drug Binding and Transport by the MDR Transporters ofJournal of fungi (Basel, Switzerland) · 2021Review
- Human ABCB1 with an ABCB11-like degenerate nucleotide binding site maintains transport activity by avoiding nucleotide occlusion.PLoS genetics · 2020Article
- Nonsynonymous Mutations in Linker-2 of the Pdr5 Multidrug Transporter Identify a New RNA Stability Element.G3 (Bethesda, Md.) · 2020Article
- Engineering endogenous ABC transporter with improving ATP supply and membrane flexibility enhances the secretion of β-carotene inBiotechnology for biofuels · 2020Article
- An A666G mutation in transmembrane helix 5 of the yeast multidrug transporter Pdr5 increases drug efflux by enhancing cooperativity between transport sites.Molecular microbiology · 2019Article
- In vitro NTPase activity of highly purified Pdr5, a major yeast ABC multidrug transporter.Scientific reports · 2019Article
- FK506 Resistance ofAntimicrobial agents and chemotherapy · 2019Article
- Robust, pleiotropic drug resistance 5 (Pdr5)-mediated multidrug resistance is vigorously maintained in Saccharomyces cerevisiae cells during glucose and nitrogen limitation.FEMS yeast research · 2018Article
- Molecular Mechanism of Taurocholate Transport by the Bile Salt Export Pump, an ABC Transporter Associated with Intrahepatic Cholestasis.Molecular pharmacology · 2017Article
- Article
- Positive regulation of the Candida albicans multidrug efflux pump Cdr1p function by phosphorylation of its N-terminal extension.The Journal of antimicrobial chemotherapy · 2016Article
- Newly identified motifs in Candida albicans Cdr1 protein nucleotide binding domains are pleiotropic drug resistance subfamily-specific and functionally asymmetric.Scientific reports · 2016Article
- Mutations of charged amino acids at the cytoplasmic end of transmembrane helix 2 affect transport activity of the budding yeast multidrug resistance protein Pdr5p.FEMS yeast research · 2016Article
- The ATPases of cohesin interface with regulators to modulate cohesin-mediated DNA tethering.eLife · 2015Article
- Mutational Analysis of Intracellular Loops Identify Cross Talk with Nucleotide Binding Domains of Yeast ABC Transporter Cdr1p.Scientific reports · 2015Article
- The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters.The Biochemical journal · 2015Review
- Evidence for a molecular diode-based mechanism in a multispecific ATP-binding cassette (ABC) exporter: SER-1368 as a gatekeeping residue in the yeast multidrug transporter Pdr5.The Journal of biological chemistry · 2014Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Pdr5 is the founding member of a large subfamily of evolutionarily distinct, clinically important fungal ABC transporters containing a characteristic, deviant ATP-binding site with altered Walker A, Walker B, Signature (C-loop), and Q-loop residues. In contrast to these motifs, the D-loops of the two ATP-binding sites have similar sequences, including a completely conserved aspartate residue. Alanine substitution mutants in the deviant Walker A and Signature motifs retain significant, albeit reduced, ATPase activity and drug resistance. The D-loop residue mutants D340A and D1042A showed a striking reduction in plasma membrane transporter levels. The D1042N mutation localized properly had nearly WT ATPase activity but was defective in transport and was profoundly hypersensitive to Pdr5 substrates. Therefore, there was a strong uncoupling of ATPase activity and drug efflux. Taken together, the properties of the mutants suggest an additional, critical intradomain signaling role for deviant ATP-binding sites.
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