Rodríguez-Alonso, R, Létoquart, J, Nguyen, VS et al. (7 more authors) (2020) Structural insight into the formation of lipoprotein-β-barrel complexes. Nature Chemical Biology, 16. pp. 1019-1025. ISSN 1552-4450
Abstract
The β-barrel assembly machinery (BAM) inserts outer membrane β-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to the cell surface by assembling RcsF–OMP complexes. Here, we report the crystal structure of the key BAM component BamA in complex with RcsF. BamA adopts an inward-open conformation, with the lateral gate to the membrane closed. RcsF is lodged deep within the lumen of the BamA barrel, binding regions proposed to undergo outward and lateral opening during OMP insertion. On the basis of our structural and biochemical data, we propose a push-and-pull model for RcsF export following conformational cycling of BamA, and provide a mechanistic explanation for how RcsF uses its interaction with BamA to detect envelope stress. Our data also suggest that the flux of incoming OMP substrates is involved in the control of BAM activity.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2020, Springer Nature. This is an author produced version of an article published in Nature Chemical Biology. Uploaded in accordance with the publisher's self-archiving policy. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | 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) > Structural Molecular Biology (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/P000037/1 BBSRC (Biotechnology & Biological Sciences Research Council) BB/M012573/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 May 2020 11:05 |
Last Modified: | 05 Jul 2022 11:14 |
Status: | Published |
Publisher: | Springer Nature |
Identification Number: | 10.1038/s41589-020-0575-0 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:160995 |