Iadanza, MG, Schiffrin, B, White, P orcid.org/0000-0001-7536-4552 et al. (9 more authors) (2020) Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs. Communications Biology, 3. 766. ISSN 2399-3642
Abstract
The β-barrel assembly machinery (BAM) catalyses the folding and insertion of β-barrel outer membrane proteins (OMPs) into the outer membranes of Gram-negative bacteria by mechanisms that remain unclear. Here, we present an ensemble of cryoEM structures of the E. coli BamABCDE (BAM) complex in lipid nanodiscs, determined using multi-body refinement techniques. These structures, supported by single-molecule FRET measurements, describe a range of motions in the BAM complex, mostly localised within the periplasmic region of the major subunit BamA. The β-barrel domain of BamA is in a ‘lateral open’ conformation in all of the determined structures, suggesting that this is the most energetically favourable species in this bilayer. Strikingly, the BAM-containing lipid nanodisc is deformed, especially around BAM’s lateral gate. This distortion is also captured in molecular dynamics simulations, and provides direct structural evidence for the lipid ‘disruptase’ activity of BAM, suggested to be an important part of its functional mechanism.
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Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Copyright © 2020, The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biomolecular Mass Spectroscopy (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Cryo EM, Image Processing (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds) The University of Leeds > Faculty of Medicine and Health (Leeds) > School of Medicine (Leeds) > Leeds Institute of Cardiovascular and Metabolic Medicine (LICAMM) > Discovery & Translational Science Dept (Leeds) |
Funding Information: | Funder Grant number Wellcome Trust 108466/Z/15/Z MRC (Medical Research Council) MR/P018491/1 BBSRC (Biotechnology & Biological Sciences Research Council) BB/N017307/1 BBSRC (Biotechnology & Biological Sciences Research Council) BB/R000271/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 Oct 2020 11:32 |
Last Modified: | 23 Feb 2021 09:00 |
Status: | Published |
Publisher: | Nature Research |
Identification Number: | 10.1038/s42003-020-01419-w |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:167025 |