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

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Caffalette, Christopher A., Corey, Robin A., Sansom, Mark S. P., Stansfeld, Phillip J. and Zimmer, Jochen (2019) A lipid gating mechanism for the channel-forming O antigen ABC transporter. Nature Communications, 10 (1). 824. doi:10.1038/s41467-019-08646-8

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Official URL: http://dx.doi.org/10.1038/s41467-019-08646-8

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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.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title: Nature Communications
Publisher: Nature Publishing Group
ISSN: 2041-1723
Official Date: 18 February 2019
Dates:
DateEvent
18 February 2019Published
23 January 2019Accepted
Volume: 10
Number: 1
Article Number: 824
DOI: 10.1038/s41467-019-08646-8
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
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