ArticleStructure (London, England : 1993)2022
In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
- Overexpression of the Multidrug Efflux Pump AcrAB-TolC in Escherichia coli for In Situ Cryo-ET Study.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A review of research progress on periplasmic adaptor proteins in bacterial tripartite pumps.Frontiers in microbiology · 2026Review
- Colistin resistance in the era of antimicrobial resistance: challenges and strategic countermeasures.Folia microbiologica · 2025Review
- Efflux-Mediated Resistance inAntibiotics (Basel, Switzerland) · 2025Review
- In situ structure and assembly of the ABC-type tripartite pump MacAB-TolC.Communications biology · 2025Article
- Structural basis of siderophore export and drug efflux by Mycobacterium tuberculosis.Nature communications · 2025Article
- The Role of the Hfq Protein in Bacterial Resistance to Antibiotics: A Narrative Review.Microorganisms · 2025Review
- A historical perspective on the multifunctional outer membrane channel protein TolC in Escherichia coli.npj antimicrobials and resistance · 2025Review
- The complex development of psoralen-interstrand crosslink resistance inbioRxiv : the preprint server for biology · 2024Article
- MgbioRxiv : the preprint server for biology · 2024Article
- Thicket and Mesh: How the Outer Membrane Can Resist Tension Imposed by the Cell Wall.The journal of physical chemistry. B · 2024Article
- A widespread single amino acid mutation in AcrA reduces tigecycline susceptibility inMicrobiology spectrum · 2024Article
- Structures and Efflux Mechanisms of the AcrAB-TolC Pump.Sub-cellular biochemistry · 2024Article
- First report of coexistence of blaKPC-2 and blaNDM-1 in carbapenem-resistant clinical isolates ofFrontiers in microbiology · 2024Article
- Role of the Bacterial Amyloid-like Hfq in Fluoroquinolone Fluxes.Microorganisms · 2023Article
- Conformational restriction shapes the inhibition of a multidrug efflux adaptor protein.Nature communications · 2023Article
- AcrAB-TolC, a major efflux pump in Gram negative bacteria: toward understanding its operation mechanism.BMB reports · 2023Review
- Antimicrobial Resistance: Two-Component Regulatory Systems and Multidrug Efflux Pumps.Antibiotics (Basel, Switzerland) · 2023Review
- Structural mass spectrometry approaches to understand multidrug efflux systems.Essays in biochemistry · 2023Review
- RND pumps across the genusMicrobial genomics · 2023Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
The tripartite AcrAB-TolC assembly, which spans both the inner and outer membranes in Gram-negative bacteria, is an efflux pump that contributes to multidrug resistance. Here, we present the in situ structure of full-length Escherichia coli AcrAB-TolC determined at 7 Å resolution by electron cryo-tomography. The TolC channel penetrates the outer membrane bilayer through to the outer leaflet and exhibits two different configurations that differ by a 60° rotation relative to the AcrB position in the pump assembly. AcrA protomers interact directly with the inner membrane and with AcrB via an interface located in proximity to the AcrB ligand-binding pocket. Our structural analysis suggests that these AcrA-bridged interactions underlie an allosteric mechanism for transmitting drug-evoked signals from AcrB to the TolC channel within the pump. Our study demonstrates the power of in situ electron cryo-tomography, which permits critical insights into the function of bacterial efflux pumps.
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Registered trials
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.