A lipid gating mechanism for the channel-forming O antigen ABC transporter

Christopher A. Caffalette, Robin A. Corey, Mark S. P. Sansom, Phillip J. Stansfeld () and Jochen Zimmer ()
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Christopher A. Caffalette: University of Virginia School of Medicine
Robin A. Corey: University of Oxford
Mark S. P. Sansom: University of Oxford
Phillip J. Stansfeld: University of Oxford
Jochen Zimmer: University of Virginia School of Medicine

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Extracellular glycan biosynthesis is a widespread microbial protection mechanism. In Gram-negative bacteria, the O antigen polysaccharide represents the variable region of outer membrane lipopolysaccharides. Fully assembled lipid-linked O antigens are translocated across the inner membrane by the WzmWzt ABC transporter for ligation to the lipopolysaccharide core, with the transporter forming a continuous transmembrane channel in a nucleotide-free state. Here, we report its structure in an ATP-bound conformation. Large structural changes within the nucleotide-binding and transmembrane regions push conserved hydrophobic residues at the substrate entry site towards the periplasm and provide a model for polysaccharide translocation. With ATP bound, the transporter forms a large transmembrane channel with openings toward the membrane and periplasm. The channel’s periplasmic exit is sealed by detergent molecules that block solvent permeation. Molecular dynamics simulation data suggest that, in a biological membrane, lipid molecules occupy this periplasmic exit and prevent water flux in the transporter’s resting state.

Date: 2019
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DOI: 10.1038/s41467-019-08646-8

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