Structural highlights
Function
A0A1T3IZT7_9FLAO
Publication Abstract from PubMed
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.
Structural basis for the pore-forming activity of a complement-like toxin.,Johnstone BA, Christie MP, Joseph R, Morton CJ, Brown HG, Hanssen E, Sanford TC, Abrahamsen HL, Tweten RK, Parker MW Sci Adv. 2025 Mar 28;11(13):eadt2127. doi: 10.1126/sciadv.adt2127. Epub 2025 Mar , 28. PMID:40153490[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Johnstone BA, Christie MP, Joseph R, Morton CJ, Brown HG, Hanssen E, Sanford TC, Abrahamsen HL, Tweten RK, Parker MW. Structural basis for the pore-forming activity of a complement-like toxin. Sci Adv. 2025 Mar 28;11(13):eadt2127. PMID:40153490 doi:10.1126/sciadv.adt2127
