ArticleNature communications2018
Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers, 1 of them a synthesis that pooled it.
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Who cites it
82 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Computer-Aided Lipase Engineering for Improving Their Stability and Activity in the Food Industry: State of the Art.Molecules (Basel, Switzerland) · 2023Pooled it
- Structural insights into a substrate translocation pathway revealed by the RND efflux pump complex MexJK fromScience advances · 2026Article
- Structure of chloramphenicol-bound MexB reveals residues in the distal binding pocket that are critical for substrate recognition.Journal of biochemistry · 2026Article
- Structural mechanisms of pump assembly and drug transport in the AcrAB-TolC efflux system.eLife · 2026Article
- Multidrug resistance transporter EmrE is only moderately sensitive to lipid composition.Biophysical journal · 2026Article
- Structural elucidation of the hexameric MmpS4-MmpL4 complex frombioRxiv : the preprint server for biology · 2026Article
- Labeling of Specific Residues of the Multidrug Transporter AcrB with Its Fluorescent Substrate.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Cloning and Characterizing Multidrug Efflux Pumps.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular basis for multidrug efflux by an anaerobic-associated RND transporter.Nature communications · 2025Article
- Strain-dependent contribution of the AcrAB-TolC efflux pump toMicrobiology (Reading, England) · 2025Article
- Fluorescein-based dyes are not valid reporters of oxidative stress in bacteria, and conclusions based on their use must be reconsidered.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Efflux pump knockout minimizes crosstalk and boosts response in transcription factor-based biosensors.Journal of biological engineering · 2025Article
- Impeding pathways of intrinsic resistance in Escherichia coli confers antibiotic sensitization and resistance proofing.PLoS biology · 2025Article
- Structural and functional analysis of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Efflux-Mediated Resistance inAntibiotics (Basel, Switzerland) · 2025Review
- Regulation, structure, and activity of theAntimicrobial agents and chemotherapy · 2025Review
- Insights into substrate recognition and export tunnel preferences in the efflux transporter AcrB.Protein science : a publication of the Protein Society · 2025Article
- Two-faced Janus SkQ1/SkQR1: patterns and molecular volume threshold for substrate recognition by the AcrAB-TolC pump.Frontiers in pharmacology · 2025Article
- Structural and functional diversity of Resistance-Nodulation-Division (RND) efflux pump transporters with implications for antimicrobial resistance.Microbiology and molecular biology reviews : MMBR · 2024Review
- Rhodamine 19 Alkyl Esters as Effective Antibacterial Agents.International journal of molecular sciences · 2024Article
22 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AcrB is the major multidrug exporter in Escherichia coli. Although several substrate-entrances have been identified, the specificity of these various transport paths remains unclear. Here we present evidence for a substrate channel (channel 3) from the central cavity of the AcrB trimer, which is connected directly to the deep pocket without first passing the switch-loop and the proximal pocket . Planar aromatic cations, such as ethidium, prefer channel 3 to channels 1 and 2. The efflux through channel 3 increases by targeted mutations and is not in competition with the export of drugs such as minocycline and erythromycin through channels 1 and 2. A switch-loop mutant, in which the pathway from the proximal to the deep pocket is hindered, can export only channel 3-utilizing drugs. The usage of multiple entrances thus contributes to the recognition and transport of a wide range of drugs with different physicochemical properties.
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