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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Pore-forming proteins, including MACPF, CDC, and gasdermin superfamilies, create large pores.
  • CDC-like proteins (CDCLs) are prevalent in gut microbes for antibacterial antagonism.
  • The structural mechanism of CDCL pore formation is currently unknown.

Purpose of the Study:

  • To elucidate the structural basis of CDCL pore formation.
  • To provide detailed structural snapshots of the CDCL pore-forming pathway.
  • To understand the regulatory features governing CDCL pore assembly.

Main Methods:

  • Crystal structure determination of a proteolytically activated CDCL.
  • Cryo-electron microscopy (cryo-EM) to resolve prepore and pore intermediates.
  • Comparative structural analysis with known pore-forming protein families.

Main Results:

  • Determined the crystal structure of an activated CDCL.
  • Obtained cryo-EM structures of a prepore-like intermediate and a transmembrane pore.
  • Revealed sophisticated regulatory features essential for productive pore formation.

Conclusions:

  • CDCLs utilize a unique mechanism to assemble giant pores.
  • The structural findings place CDCLs within the continuum of MACPF, CDC, and gasdermin pore superfamilies.
  • This work clarifies the structural underpinnings of CDCL-mediated antibacterial antagonism.