Conformational investigation of the asymmetric periplasmic domains of E. coli LptB₂FGC using SDSL CW EPR spectroscopy.

ABSTRACT: The majority of pathogenic Gram-negative bacteria benefit from intrinsic antibiotic resistance, attributed primarily to the lipopolysaccharide (LPS) coating of the bacterial envelope. To effectively coat the bacterial cell envelope, LPS is transported from the inner membrane by the LPS transport (Lpt) system, which comprises seven distinct Lpt proteins, LptA-G, that form a stable protein bridge spanning the periplasm to connect the inner and outer membranes. The driving force of this process, LptB₂FG, is an asymmetric ATP binding cassette (ABC) transporter with a novel architecture and function that ejects LPS from the inner membrane and facilitates transfer to the periplasmic bridge. Here, we utilize site-directed spin labeling (SDSL) electron paramagnetic resonance (EPR) spect

SUBMITTER: Cina NP 

PROVIDER: S-EPMC11025719 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature