ArticleNature communications2016
Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 63 citations in OpenAlex.
- Structural insights into a substrate translocation pathway revealed by the RND efflux pump complex MexJK fromScience advances · 2026Article
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- Computer Simulations of Multidrug Efflux Pumps of the Resistance-Nodulation-Cell Division Superfamily.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- A novel role for colistin as an efflux pump inhibitor in multidrug-resistant Klebsiella pneumoniae.Scientific reports · 2025Article
- Mechanisms of fusidic acid resistance.Biochemical Society transactions · 2025Review
- Efflux-Mediated Resistance inAntibiotics (Basel, Switzerland) · 2025Review
- Two-faced Janus SkQ1/SkQR1: patterns and molecular volume threshold for substrate recognition by the AcrAB-TolC pump.Frontiers in pharmacology · 2025Article
- Insights into substrate recognition and export tunnel preferences in the efflux transporter AcrB.Protein science : a publication of the Protein Society · 2025Article
- Molecular insights into the determinants of substrate specificity and efflux inhibition of the RND efflux pumps AcrB and AdeB.Microbiology (Reading, England) · 2024Review
- The Art of War withAntibiotics (Basel, Switzerland) · 2023Review
- AcrAB-TolC, a major efflux pump in Gram negative bacteria: toward understanding its operation mechanism.BMB reports · 2023Review
- Molecular mechanisms of antibiotic resistance revisited.Nature reviews. Microbiology · 2023Review
- Tripartite efflux pumps of the RND superfamily: what did we learn from computational studies?Microbiology (Reading, England) · 2023Review
- Update on the Discovery of Efflux Pump Inhibitors against Critical Priority Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Spatial Characteristics of the Efflux Pump MexB Determine Inhibitor Binding.Antimicrobial agents and chemotherapy · 2022Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Recognition of quinolone antibiotics by the multidrug efflux transporter MexB ofPhysical chemistry chemical physics : PCCP · 2022Article
- Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps.Nature communications · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The deployment of multidrug efflux pumps is a powerful defence mechanism for Gram-negative bacterial cells when exposed to antimicrobial agents. The major multidrug efflux transport system in Escherichia coli, AcrAB-TolC, is a tripartite system using the proton-motive force as an energy source. The polyspecific substrate-binding module AcrB uses various pathways to sequester drugs from the periplasm and outer leaflet of the inner membrane. Here we report the asymmetric AcrB structure in complex with fusidic acid at a resolution of 2.5 Å and mutational analysis of the putative fusidic acid binding site at the transmembrane domain. A groove shaped by the interface between transmembrane helix 1 (TM1) and TM2 specifically binds fusidic acid and other lipophilic carboxylated drugs. We propose that these bound drugs are actively displaced by an upward movement of TM2 towards the AcrB periplasmic porter domain in response to protonation events in the transmembrane domain.
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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.