Structure of a full-length bacterial polysaccharide co-polymerase.

Wiseman B, Nitharwal RG, Widmalm G, Högbom M

Nat Commun 12 (1) 369 [2021-01-14; online 2021-01-14]

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.

Cryo-EM [Service]

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PubMed 33446644

DOI 10.1038/s41467-020-20579-1

Crossref 10.1038/s41467-020-20579-1

pii: 10.1038/s41467-020-20579-1
pmc: PMC7809406