9CCP

Cryo-EM structure of the EaCDCL pore

This is a non-PDB format compatible entry.

Summary for 9CCP

• Entry DOI: 10.2210/pdb9ccp/pdb
• EMDB information: 45451
• Descriptor: Thiol-activated cytolysin family protein, CALCIUM ION (2 entities in total)
• Functional Keywords: pore-forming toxin, cholesterol-dependent cytolysin like, elizabethkingia anophelis, macpf, complement, toxin
• Biological source: Elizabethkingia anophelis Ag1
• Total number of polymer chains: 30
• Total formula weight: 1186023.75

Authors

Johnstone, B.A.,Christie, M.P.,Morton, C.M.,Brown, H.G.,Hanssen, E.,Parker, M.W. (deposition date: 2024-06-23, release date: 2025-04-09)

Primary citation

Johnstone, B.A.,Christie, M.P.,Joseph, R.,Morton, C.J.,Brown, H.G.,Hanssen, E.,Sanford, T.C.,Abrahamsen, H.L.,Tweten, R.K.,Parker, M.W.
Structural basis for the pore-forming activity of a complement-like toxin.
Sci Adv, 11:eadt2127-eadt2127, 2025

PubMed Abstract: Pore-forming proteins comprise a highly diverse group of proteins exemplified by the membrane attack complex/perforin (MACPF), cholesterol-dependent cytolysin (CDC), and gasdermin superfamilies, which all form gigantic pores (>150 angstroms). A recently found family of pore-forming toxins, called CDC-like proteins (CDCLs), are wide-spread in gut microbes and are a prevalent means of antibacterial antagonism. However, the structural aspects of how CDCLs assemble a pore remain a mystery. Here, we report the crystal structure of a proteolytically activated CDCL and cryo-electron microscopy structures of a prepore-like intermediate and a transmembrane pore providing detailed snapshots across the entire pore-forming pathway. These studies reveal a sophisticated array of regulatory features to ensure productive pore formation, and, thus, CDCLs straddle the MACPF, CDC, and gasdermin lineages of the giant pore superfamilies.

PubMed: 40153490
DOI: 10.1126/sciadv.adt2127

Experimental method

ELECTRON MICROSCOPY (2.87 Å)