Lipopolysaccharide transport involves long-range coupling between cytoplasmic and periplasmic domains of the LptB₂FGC extractor.

ABSTRACT: The cell surface of the Gram-negative cell envelope contains lipopolysaccharide (LPS) molecules, which form a permeability barrier against hydrophobic antibiotics. The LPS transport (Lpt) machine composed of LptB₂FGCADE forms a proteinaceous trans-envelope bridge that allows for the rapid and specific transport of newly synthesized LPS from the inner membrane (IM) to the outer membrane (OM). This transport is powered from the IM by the ATP-binding cassette transporter LptB₂FGC. The ATP-driven cycling between closed- and open-dimer states of the ATPase LptB₂ is coupled to the extraction of LPS by the transmembrane domains LptFG. However, the mechanism by which LPS moves from a substrate-binding cavity formed by LptFG at the IM to the first component of the p

SUBMITTER: Lundstedt EA 

PROVIDER: S-EPMC8095461 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature