These structures reveal how multiple regulatory features, such as proteolytic activation, ensure pore formation. Furthermore, we find features that are not common to the related CDC family of pore-forming toxins. Instead, CDCLs seem show features that straddle the CDC, MACPF and gasdermin families.

This includes the crystal structure of the proteolytically-activated form and cryo-EM structures of the inserted pore and prepore-like complex, solved on the surface of liposomes.

Excited to share that our work on a family of pore-forming proteins is now live in Science Advances! We show structural snapshots across the entire pore-forming pathway for a cholesterol-dependent cytolysin-like (CDCL) bicomponent system.