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Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism

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Khera,  Radhika
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mehdipour,  Ahmad Reza
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Centre for molecular modelling, Ghent University, Zwijnaarde, Belgium;

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Welsch,  Sonja       
Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Münke,  Cornelia
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hummer,  Gerhard       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany;

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Xie,  Hao       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Khera, R., Mehdipour, A. R., Bolla, J. R., Kahnt, J., Welsch, S., Ermler, U., et al. (2022). Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism. The EMBO Journal, 41(18): e109990. doi:10.15252/embj.2021109990.


Cite as: https://hdl.handle.net/21.11116/0000-000A-9926-F
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.