Structures of LolB bound to LolA or lipoprotein provide insight into the final steps of bacterial lipoprotein trafficking

Atomic structures of LolB bound to LolA and to a lipoprotein reveal how LolB’s protruding loop and a molecular latch coordinate substrate transfer at the Gram-negative outer membrane.

• Why it matters: The Lol system is crucial for moving triacylated lipoproteins from the inner membrane to the outer membrane, making the LolB–LolA handoff a key step for envelope function and antimicrobial targeting.
• What they did: The authors solved LolB–LolA and lipoprotein-bound LolB complexes and validated them with in vivo and in vitro assays, using biophysical measurements to define how positively charged LolB residues and a latch release the LolA cavity lid.
• The result: The structures, supported by biophysics and modelling onto predicted LolB orientations, provide a rationale for LolA release and triacyl group insertion, elucidating two terminal trafficking intermediates.

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