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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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WRAP-A-lipid-gating-mechanism-channel-forming-O-antigen-ABC-transporter-Stansfeld-2019.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2730Kb) | Preview |
Official URL: http://dx.doi.org/10.1038/s41467-019-08646-8
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 | ||||||
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| Divisions: | Faculty of Science > Life Sciences (2010- ) | ||||||
| Journal or Publication Title: | Nature Communications | ||||||
| Publisher: | Nature Publishing Group | ||||||
| ISSN: | 2041-1723 | ||||||
| Official Date: | 18 February 2019 | ||||||
| Dates: |
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| 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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