ArticleFrontiers in molecular biosciences2020
Mutations in the TolC Periplasmic Domain Affect Substrate Specificity of the AcrAB-TolC Pump.
Article in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Structural mechanisms of pump assembly and drug transport in the AcrAB-TolC efflux system.eLife · 2026Article
- Genomic analysis reveals multi-level resistance network linking oxidative stress pathway mutations to cefiderocol resistance and clonal evolution inFrontiers in cellular and infection microbiology · 2026Article
- The Resistance-Nodulation-Division efflux pump EefABC is highly conserved within lineages ofMicrobial genomics · 2026Article
- A historical perspective on the multifunctional outer membrane channel protein TolC in Escherichia coli.npj antimicrobials and resistance · 2025Review
- Structural shifts in TolC facilitate Efflux-Mediated β-lactam resistance.Communications biology · 2024Article
- Discovery and Characterization of Two Folded Intermediates for Outer Membrane Protein TolC Biogenesis.Journal of molecular biology · 2024Article
- The Properties of Linezolid, Rifampicin, and Vancomycin, as Well as the Mechanism of Action of Pentamidine, Determine Their Synergy against Gram-Negative Bacteria.International journal of molecular sciences · 2023Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- Molecular Determinants for OMF Selectivity in Tripartite RND Multidrug Efflux Systems.Antibiotics (Basel, Switzerland) · 2022Article
- Common recognition topology of mex transporters ofFrontiers in pharmacology · 2022Article
- Lpp positions peptidoglycan at the AcrA-TolC interface in the AcrAB-TolC multidrug efflux pump.Biophysical journal · 2021Article
- Insight into the AcrAB-TolC Complex Assembly Process Learned from Competition Studies.Antibiotics (Basel, Switzerland) · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TolC and the other members of the outer membrane factor (OMF) family are outer membrane proteins forming trimeric channels that serve as a conduit for most actively effluxed substrates in Gram-negative bacteria by providing a key component in a multitude of tripartite efflux-pumps. Current models of tripartite pump assembly ascribe substrate selection to the inner-membrane transporter and periplasmic-adapter protein (PAP) assembly, suggesting that TolC is a passive, non-selective channel. While the membrane-embedded portion of the protein adopts a porin-like fold, the periplasmic domain of TolC presents a unique "alpha-barrel" architecture. This alpha-barrel consists of pseudo-continuous α-helices forming curved coiled-coils, whose tips form α-helical hairpins, relaxation of which results in a transition of TolC from a closed to an open-aperture state allowing effective efflux of substrates through its channel. Here, we analyzed the effects of site-directed mutations targeting the alpha-barrel of TolC, of the principal tripartite efflux-pump
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