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Structural insight into the formation of lipoprotein-β-barrel complexes

DOI: 10.1038/s41589-020-0575-0 DOI Help

Authors: Raquel Rodriguez-alonso (Walloon Excellence in Life Sciences and Biotechnology; de Duve Institute, Université Catholique de Louvain) , Juliette Letoquart (Walloon Excellence in Life Sciences and Biotechnology; de Duve Institute, Université Catholique de Louvain) , Van Son Nguyen (Vrije Universiteit Brussel; VIB) , Gwennaelle Louis (Walloon Excellence in Life Sciences and Biotechnology; de Duve Institute, Université Catholique de Louvain) , Antonio N. Calabrese (University of Leeds) , Bogdan I. Iorga (de Duve Institute, Université Catholique de Louvain; Université Paris-Saclay) , Sheena E. Radford (University of Leeds) , Seung-hyun Cho (Walloon Excellence in Life Sciences and Biotechnology; de Duve Institute, Université Catholique de Louvain) , Han Remaut (Vrije Universiteit Brussel; VIB) , Jean-françois Collet (Walloon Excellence in Life Sciences and Biotechnology; de Duve Institute, Université Catholique de Louvain)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Chemical Biology , VOL 15

State: Published (Approved)
Published: June 2020
Diamond Proposal Number(s): 17150

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.

Journal Keywords: Bacteria; Membrane proteins; X-ray crystallography

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: Soleil Synchrotron