Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs

Author:

Iadanza Matthew G.,Schiffrin Bob,White Paul,Watson Matthew A.,Horne Jim E.,Higgins Anna J.,Calabrese Antonio N.ORCID,Brockwell David J.ORCID,Tuma RomanORCID,Kalli Antreas C.ORCID,Radford Sheena E.ORCID,Ranson Neil A.ORCID

Abstract

AbstractThe 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.

Publisher

Springer Science and Business Media LLC

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology,Medicine (miscellaneous)

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