Substrate-induced asymmetry coordinates lipoprotein handover and abaucin trapping in Acinetobacter baumannii LolDF

Substrate binding to homodimeric LolDF in Acinetobacter baumannii breaks LolF symmetry, with LolFB mainly binding the lipid anchor and LolFA positioning the adjacent polypeptide.

• Why it matters: Directional lipoprotein transport by homodimeric LolDF and how the reported two- and four-abaucin states relate were unclear, limiting a unified model of productive handover versus inhibition.
• What they did: Using defined lipidated AbLolB and AbLolA, the authors mapped substrate-induced asymmetry and compared abaucin-bound structures by C1 reconstruction of the wide state versus C2 processing that averages asymmetry.
• The result: Abaucin inhibits ATPase activity and LolA-mediated transfer from substrate-associated LolDF, and the wide-state structure implies non-equivalent central ligands that become averaged during processing.

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