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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The bacterial tight adherence pilus system (TadPS) is crucial for pathogen adhesion and colonization.
  • Pilus assembly and dynamics are driven by the ATPase CpaF (TadA), but its mechanism remains unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of CpaF (TadA) in powering TadPS pilus dynamics.
  • To characterize the structural basis for CpaF's ATPase activity and conformational changes.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) to determine CpaF structure in different nucleotide states.
  • Cell-based light microscopy to assess the in vivo function of CpaF mutants.
  • Biochemical assays to study nucleotide cycling and conformational changes.

Main Results:

  • CpaF (TadA) forms a hexamer with C2 symmetry, undergoing nucleotide-dependent conformational changes.
  • Nucleotide cycling involves an intra-subunit clamp-like mechanism, driving sequential subunit alterations.
  • Mutational analysis identified key residues involved in CpaF interaction with platform proteins (CpaG/TadB, CpaH/TadC).

Conclusions:

  • A model for CpaF (TadA) driven bidirectional pilus motion is proposed.
  • Understanding CpaF mechanism provides insights into the broader family of type 4 filament assembly ATPases.
  • This work has implications for targeting bacterial adhesion mechanisms in human pathogens.