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


Journal

The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664

Informations de publication

Date de publication:
15 09 2022
Historique:
revised: 04 05 2022
received: 20 10 2021
accepted: 06 05 2022
pubmed: 15 6 2022
medline: 17 9 2022
entrez: 14 6 2022
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 35698912
doi: 10.15252/embj.2021109990
pmc: PMC9475539
doi:

Substances chimiques

Bacterial Proteins 0
Lactones 0
N-octanoylhomoserine lactone 0
Homoserine 6KA95X0IVO

Banques de données

PDB
['7NB6', '7OT9']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e109990

Informations de copyright

© 2022 The Authors. Published under the terms of the CC BY NC ND 4.0 license.

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Auteurs

Radhika Khera (R)

Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

Ahmad R Mehdipour (AR)

Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Centre for molecular modelling, Ghent University, Zwijnaarde, Belgium.

Jani R Bolla (JR)

Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
The Kavli Institute for Nanoscience Discovery, Oxford, UK.
Department of Plant Sciences, University of Oxford, Oxford, UK.

Joerg Kahnt (J)

Core Facility for Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.

Sonja Welsch (S)

Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

Ulrich Ermler (U)

Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

Cornelia Muenke (C)

Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

Carol V Robinson (CV)

Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK.
The Kavli Institute for Nanoscience Discovery, Oxford, UK.

Gerhard Hummer (G)

Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany.

Hao Xie (H)

Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

Hartmut Michel (H)

Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

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Classifications MeSH