The transmembrane α-helix of LptC participates in LPS extraction by the LptB₂ FGC transporter.

ABSTRACT: Lipopolysaccharide (LPS) is an essential component of the outer membrane of most Gram-negative bacteria that provides resistance to various toxic compounds and antibiotics. Newly synthesized LPS is extracted from the inner membrane by the ATP-binding cassette (ABC) transporter LptB₂ FGC, which places the glycolipid onto a periplasmic protein bridge that connects to the outer membrane. This ABC transporter is structurally unusual in that it associates with an additional protein, LptC. The periplasmic domain of LptC is part of the transporter's bridge while its transmembrane α-helix intercalates into the LPS-binding cavity of the core LptB₂ FG transporter. LptC's transmembrane helix affects the in vitro ATPase activity of LptB₂ FG, but its role in LPS transpo

SUBMITTER: Wilson A 

PROVIDER: S-EPMC9544173 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature