ArticleThe EMBO journal2022
Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism.
Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Discovery of dietary polyphenols targeting the autoinducer-2 quorum sensing system of pathogenic bacteria.Gut microbes · 2026Article
- Repurposing loratadine to reverse colistin resistance inEmerging microbes & infections · 2026Article
- Targeting Quorum Sensing to Combat Foodborne Pathogens: A Dual Strategy Against Spoilage and Pathogenesis.Foods (Basel, Switzerland) · 2026Review
- Less is more: the lack of autoinducer-2-dependent quorum sensing promotes competitive fitness ofFrontiers in cellular and infection microbiology · 2025Article
- Campylobacter jejuni virulence factors: update on emerging issues and trends.Journal of biomedical science · 2024Review
- Discovery of AI-2 Quorum Sensing Inhibitors Targeting the LsrK/HPr Protein-Protein Interaction Site by Molecular Dynamics Simulation, Virtual Screening, and Bioassay Evaluation.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Mass spectrometry of intact membrane proteins: shifting towards a more native-like context.Essays in biochemistry · 2023Review
- Quorum sensing componentry opens new lines of communication.The EMBO journal · 2022Article
- Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism.The EMBO journal · 2022Article
- Assembly and Functional Role of PACE Transporter PA2880 from Pseudomonas aeruginosa.Microbiology spectrum · 2022Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria utilize small extracellular molecules to communicate in order to collectively coordinate their behaviors in response to the population density. Autoinducer-2 (AI-2), a universal molecule for both intra- and inter-species communication, is involved in the regulation of biofilm formation, virulence, motility, chemotaxis, and antibiotic resistance. While many studies have been devoted to understanding the biosynthesis and sensing of AI-2, very little information is available on its export. The protein TqsA from Escherichia coli, which belongs to the AI-2 exporter superfamily, has been shown to export AI-2. Here, we report the cryogenic electron microscopic structures of two AI-2 exporters (TqsA and YdiK) from E. coli at 3.35 Å and 2.80 Å resolutions, respectively. Our structures suggest that the AI-2 exporter exists as a homo-pentameric complex. In silico molecular docking and native mass spectrometry experiments were employed to demonstrate the interaction between AI-2 and TqsA, and the results highlight the functional importance of two helical hairpins in substrate binding. We propose that each monomer works as an independent functional unit utilizing an elevator-type transport mechanism.
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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.