Details

Autor(en) / Beteiligte

• Li, Yanyan
• Orlando, Benjamin J
• Liao, Maofu

Titel

Structural basis of lipopolysaccharide extraction by the LptB 2 FGC complex

Ist Teil von

• Nature (London), 2019-03, Vol.567 (7749), p.486

Ort / Verlag

England

Erscheinungsjahr

2019

Quelle

MEDLINE

Beschreibungen/Notizen

• In Gram-negative bacteria, lipopolysaccharide is essential for outer membrane formation and antibiotic resistance. The seven lipopolysaccharide transport (Lpt) proteins A-G move lipopolysaccharide from the inner to the outer membrane. The ATP-binding cassette transporter LptB FG, which tightly associates with LptC, extracts lipopolysaccharide out of the inner membrane. The mechanism of the LptB FG-LptC complex (LptB FGC) and the role of LptC in lipopolysaccharide transport are poorly understood. Here we characterize the structures of LptB FG and LptB FGC in nucleotide-free and vanadate-trapped states, using single-particle cryo-electron microscopy. These structures resolve the bound lipopolysaccharide, reveal transporter-lipopolysaccharide interactions with side-chain details and uncover how the capture and extrusion of lipopolysaccharide are coupled to conformational rearrangements of LptB FGC. LptC inserts its transmembrane helix between the two transmembrane domains of LptB FG, which represents a previously unknown regulatory mechanism for ATP-binding cassette transporters. Our results suggest a role for LptC in achieving efficient lipopolysaccharide transport, by coordinating the action of LptB FG in the inner membrane and Lpt protein interactions in the periplasm.