6rbg

Publication Abstract from PubMed

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 A 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 A 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.

Structure of a full-length bacterial polysaccharide co-polymerase.,Wiseman B, Nitharwal RG, Widmalm G, Hogbom M Nat Commun. 2021 Jan 14;12(1):369. doi: 10.1038/s41467-020-20579-1. PMID:33446644^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.