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TitleStructural basis for the pore-forming activity of a complement-like toxin.
Journal, issue, pagesSci Adv, Vol. 11, Issue 13, Page eadt2127, Year 2025
Publish dateMar 28, 2025
AuthorsBronte A Johnstone / Michelle P Christie / Riya Joseph / Craig J Morton / Hamish G Brown / Eric Hanssen / Tristan C Sanford / Hunter L Abrahamsen / Rodney K Tweten / Michael W Parker /
PubMed AbstractPore-forming proteins comprise a highly diverse group of proteins exemplified by the membrane attack complex/perforin (MACPF), cholesterol-dependent cytolysin (CDC), and gasdermin superfamilies, ...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.
External linksSci Adv / PubMed:40153490 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.49 - 6.5 Å
Structure data

EMDB-45448: Double-stacked pore and prepore-like complex (C1 symmetry)
Method: EM (single particle) / Resolution: 3.35 Å

EMDB-45449: Double-stacked pore and prepore-like complex (C30 symmetry)
Method: EM (single particle) / Resolution: 2.97 Å

EMDB-45450: EaCDCL pore complex (C1 symmetry)
Method: EM (single particle) / Resolution: 3.43 Å

45451

9ccp

EMDB-45451, PDB-9ccp:
Cryo-EM structure of the EaCDCL pore
Method: EM (single particle) / Resolution: 2.87 Å

EMDB-45452: Prepore-like EaCDCL short oligomer (C1 symmetry)
Method: EM (single particle) / Resolution: 3.52 Å

45453

9ccq

EMDB-45453, PDB-9ccq:
Cryo-EM structure of the prepore-like EaCDCL short oligomer
Method: EM (single particle) / Resolution: 3.13 Å

EMDB-45454: EaCDCL pore complex, non-stacked control (C1)
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-45455: EaCDCL pore complex, non-stacked control (C30 symmetry)
Method: EM (single particle) / Resolution: 3.44 Å

PDB-8g33:
Activated form of a CDCL long protein
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

Source
  • elizabethkingia anophelis ag1 (bacteria)
KeywordsTOXIN / Pore-forming toxin / cholesterol-dependent cytolysin like / Elizabethkingia anophelis / MACPF / complement

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