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Cryo-EM Reveals LptM’s Key Role in Stabilizing Bacterial LptDE Complex

Detailed in an online preprint since July 16, these results illuminate how the Lpt system builds bacterial outer membranes to inform antibiotic design.

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Overview

  • A preprint posted on July 16 shows that LptM binds a folded LptD intermediate through a segment of fewer than ten amino acids to stabilize the LptDE complex.
  • Cryo-electron microscopy provides a high-resolution view of the LptM–LptDE interface in Escherichia coli.
  • LptM’s late-stage role fine-tunes LptD maturation and secures lipopolysaccharide transport across the outer membrane.
  • Mutational analysis pinpoints the essential amino-acid motif within LptM responsible for its stabilizing function.
  • These insights position the LptDE translocon as a compelling target for novel antibiotics against resistant Gram-negative bacteria.