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- W3124082014 abstract "Lipopolysaccharides are important components of the bacterial cell envelope that among other things act as a protective barrier against the environment and toxic molecules such as antibiotics. One of the most widely disseminated pathways of polysaccharide biosynthesis is the inner membrane bound Wzy-dependent pathway. Here we present the 3.0 Å structure of the co-polymerase component of this pathway, WzzB from E. coli solved by single-particle cryo-electron microscopy. The overall architecture is octameric and resembles a box jellyfish containing a large bell-shaped periplasmic domain with the 2-helix transmembrane domain from each protomer, positioned 32 Å apart, encircling a large empty transmembrane chamber. This structure also reveals the architecture of the transmembrane domain, including the location of key residues for the Wzz-family of proteins and the Wzy-dependent pathway present in many Gram-negative bacteria, explaining several of the previous biochemical and mutational studies and lays the foundation for future investigations." @default.
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- W3124082014 date "2021-01-14" @default.
- W3124082014 modified "2023-10-17" @default.
- W3124082014 title "Structure of a full-length bacterial polysaccharide co-polymerase" @default.
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- W3124082014 doi "https://doi.org/10.1038/s41467-020-20579-1" @default.
- W3124082014 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7809406" @default.
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