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Multiple conformations facilitate PilT function in the type IV pilus.

Matthew McCallum1,2, Samir Benlekbir2, Sheryl Nguyen2

  • 1Department of Biochemistry, University of Toronto, Toronto, ON, M5S 1A8, Canada.

Nature Communications
|November 16, 2019
PubMed
Summary
This summary is machine-generated.

Type IV pilus systems use motor ATPases like PilT for bacterial virulence. This study reveals how PilT adopts different conformations (C2, C3, C6), crucial for its function in pilus assembly.

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Area of Science:

  • Bacteriology
  • Structural Biology
  • Molecular Motors

Background:

  • Type IV pilus systems are essential for bacterial pathogenesis, mediating adhesion and motility.
  • Pilin polymerization/depolymerization is driven by PilT/VirB11-like motor ATPases.
  • The functional relevance of observed C3/C6 conformations versus the proposed C2 symmetry remains unclear.

Purpose of the Study:

  • To elucidate the structural conformations of PilT and their functional significance.
  • To classify the conformational states of related PilT/VirB11-like ATPases.
  • To develop a comprehensive model for PilT function.

Main Methods:

  • X-ray crystallography to determine PilT structures in multiple conformations.
  • Single particle electron cryomicroscopy (cryo-EM) to analyze conformational preferences.
  • Coevolution analysis and functional studies of point mutants.

Main Results:

  • PilT exhibits condition-dependent preferences for C2, C3, and C6 conformations.
  • Structural data allowed classification of various PilT/VirB11-like family member structures.
  • Functional studies identified a gain-of-function mutation favoring the C2 conformation.

Conclusions:

  • Multiple conformations (C2, C3, C6) are physiologically relevant for PilT function.
  • A new model for PilT function provides insights into the broader PilT/VirB11-like ATPase family.
  • Understanding these conformations is key to targeting bacterial virulence mechanisms.