ArticleMolecules and cells2015
Structure of the tripartite multidrug efflux pump AcrAB-TolC suggests an alternative assembly mode.
Article in Molecules and cells, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- A hidden reservoir of antibiotic resistance genes: transferable plasmids in community air and wastewater.Frontiers in microbiology · 2026Article
- Labeling of Specific Residues of the Multidrug Transporter AcrB with Its Fluorescent Substrate.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- Article
- Characterization ofFrontiers in cellular and infection microbiology · 2025Article
- A robust protocol for refolding TolC and other outer membrane components of tripartite efflux pumps from inclusion bodies.Methods in enzymology · 2025Article
- MgbioRxiv : the preprint server for biology · 2024Article
- Article
- Molecular insights into the determinants of substrate specificity and efflux inhibition of the RND efflux pumps AcrB and AdeB.Microbiology (Reading, England) · 2024Review
- Inhibition of AcrAB-TolC enhances antimicrobial activity of phytochemicals inFrontiers in plant science · 2023Article
- Molecular rationale for the impairment of the MexAB-OprM efflux pump by a single mutation in MexA.Computational and structural biotechnology journal · 2022Article
- Lpp positions peptidoglycan at the AcrA-TolC interface in the AcrAB-TolC multidrug efflux pump.Biophysical journal · 2021Article
- Ever-Adapting RND Efflux Pumps in Gram-Negative Multidrug-Resistant Pathogens: A Race against Time.Antibiotics (Basel, Switzerland) · 2021Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Periplasmic Targets for the Development of Effective Antimicrobials against Gram-Negative Bacteria.ACS infectious diseases · 2020Review
- Probing the Dynamics of AcrB Through Disulfide Bond Formation.ACS omega · 2020Article
- Mutations in the TolC Periplasmic Domain Affect Substrate Specificity of the AcrAB-TolC Pump.Frontiers in molecular biosciences · 2020Article
- Crystal Structure of the Regulatory Domain of MexT, a Transcriptional Activator of the MexEFOprN Efflux Pump inMolecules and cells · 2019Article
- Conformational Dynamics of AcrA Govern Multidrug Efflux Pump Assembly.ACS infectious diseases · 2019Article
- In situ structure and assembly of the multidrug efflux pump AcrAB-TolC.Nature communications · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli AcrAB-TolC is a multidrug efflux pump that expels a wide range of toxic substrates. The dynamic nature of the binding or low affinity between the components has impeded elucidation of how the three components assemble in the functional state. Here, we created fusion proteins composed of AcrB, a transmembrane linker, and two copies of AcrA. The fusion protein exhibited acridine pumping activity, suggesting that the protein reflects the functional structure in vivo. To discern the assembling mode with TolC, the AcrBA fusion protein was incubated with TolC or a chimeric protein containing the TolC aperture tip region. Three-dimensional structures of the complex proteins were determined through transmission electron microscopy. The overall structure exemplifies the adaptor bridging model, wherein the funnel-like AcrA hexamer forms an intermeshing cogwheel interaction with the α-barrel tip region of TolC, and a direct interaction between AcrB and TolC is not allowed. These observations provide a structural blueprint for understanding multidrug resistance in pathogenic Gram-negative bacteria.
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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.