Summary for 8G33
| Entry DOI | 10.2210/pdb8g33/pdb |
| Descriptor | Hemolysin (2 entities in total) |
| Functional Keywords | pore-forming toxin, cholesterol-dependent cytolysin like, elizabethkingia anophelis, toxin |
| Biological source | Elizabethkingia anophelis Ag1 |
| Total number of polymer chains | 1 |
| Total formula weight | 55906.49 |
| Authors | Johnstone, B.A.,Christie, M.P.,Morton, C.J.,Parker, M.W. (deposition date: 2023-02-06, release date: 2024-02-07, Last modification 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 Cited by 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: 40153490DOI: 10.1126/sciadv.adt2127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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