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• W2913394885 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." @default.
• W2913394885 created "2019-02-21" @default.
• W2913394885 creator A5013028120 @default.
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• W2913394885 date "2019-02-18" @default.
• W2913394885 modified "2023-10-13" @default.
• W2913394885 title "A lipid gating mechanism for the channel-forming O antigen ABC transporter" @default.
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• W2913394885 doi "https://doi.org/10.1038/s41467-019-08646-8" @default.
• W2913394885 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6379404" @default.
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• W2913394885 hasPublicationYear "2019" @default.
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