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Outer membrane protein assembly mediated by BAM-SurA complexes.

Katherine L Fenn1, Jim E Horne1,2, Joel A Crossley1

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The Gram-negative bacterial outer membrane is crucial for protection.
  • Outer membrane protein (OMP) insertion relies on the β-barrel assembly machinery (BAM).
  • The periplasmic chaperone SurA delivers unfolded OMPs to BAM, but the mechanism is unclear.

Purpose of the Study:

  • To elucidate the mechanism of SurA-mediated OMP delivery to BAM.
  • To understand the structural basis of SurA-BAM interaction for OMP biogenesis.

Main Methods:

  • Disulphide bond engineering to trap SurA-BAM complexes.
  • Cryo-electron microscopy (cryo-EM) to solve complex structures.
  • AlphaFold2 modeling to guide experiments.

Main Results:

  • SurA binds BAM at the POTRA-1 domain, inducing conformational changes.
  • OMP transfer to the BAM lateral gate is facilitated by SurA-BAM interaction.
  • Disruption of SurA-BAM interaction causes outer membrane assembly defects.

Conclusions:

  • SurA plays a critical role in outer membrane biogenesis by mediating OMP transfer to BAM.
  • The SurA-BAM interaction is essential for bacterial outer membrane integrity.
  • Structural insights into SurA-BAM complex formation advance understanding of OMP insertion.