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Related Experiment Videos

Structural basis of chaperone function and pilus biogenesis.

F G Sauer1, K Fütterer, J S Pinkner

  • 1Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.

Science (New York, N.Y.)
|August 14, 1999
PubMed
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Gram-negative pathogens use the chaperone-usher pathway to build adhesive pili. Chaperones donate beta strands to subunits, enabling pilus assembly through donor strand complementation and exchange.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gram-negative pathogens utilize the chaperone-usher pathway for pilus biogenesis.
  • Adhesive pili are crucial for bacterial adhesion and virulence.
  • This pathway involves periplasmic chaperones and outer membrane usher complexes.

Purpose of the Study:

  • To elucidate the structural mechanisms of pilus subunit assembly.
  • To understand the role of chaperones in the chaperone-usher pathway.
  • To provide insights into the biogenesis of Gram-negative bacterial pili.

Main Methods:

  • X-ray crystallography was used to determine the structure of the PapD-PapK chaperone-subunit complex.
  • High-resolution structural analysis at 2.4 angstrom.

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Main Results:

  • The crystal structure reveals the chaperone (PapD) donates a G(1) beta strand to complete the immunoglobulin-like fold of the pilus subunit (PapK).
  • This process is termed donor strand complementation.
  • The structure also suggests a mechanism of donor strand exchange for pilus elongation during biogenesis.

Conclusions:

  • The chaperone-usher pathway employs donor strand complementation for initial subunit folding.
  • Donor strand exchange is likely involved in the sequential assembly of pilus subunits.
  • Structural insights advance our understanding of bacterial adhesion and potential therapeutic targets.