LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope

摘要

Gram-negative bacteria are surrounded by an outer membrane composed of phospholipids and lipopolysaccharide, which acts as a barrier and contributes to antibiotic resistance. The systems that mediate phospholipid trafficking across the periplasm, such as MCE (Mammalian Cell Entry) transporters, have not been well characterized. Our similar to 3.5 angstrom cryo-EM structure of the E. coli MCE protein LetB reveals an similar to 0.6 megadalton complex that consists of seven stacked rings, with a central hydrophobic tunnel sufficiently long to span the perk plasm. Lipids bind inside the tunnel, suggesting that it functions as a pathway for lipid transport. Cryo-EM structures in the open and closed states reveal a dynamic tunnel lining, with implications for gating or substrate translocation. Our results support a model in which LetB establishes a physical link between the two membranes and creates a hydrophobic pathway for the translocation of lipids across the periplasm.