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Structure paper

TitleElucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.
Journal, issue, pagesSci Adv, Vol. 11, Issue 39, Page eadv0683, Year 2025
Publish dateSep 26, 2025
AuthorsRocío Arranz / César Santiago / Simonas Masiulis / Esperanza Rivera-de-Torre / Juan Palacios-Ortega / Diego Carlero / Diego Heras-Márquez / José G Gavilanes / Ernesto Arias-Palomo / Álvaro Martínez-Del-Pozo / Sara García-Linares / Jaime Martín-Benito /
PubMed AbstractPore-forming proteins exemplify the transformative potential of biological molecules. Produced as soluble monomers, they assemble into multimeric membrane-inserted complexes in response to specific ...Pore-forming proteins exemplify the transformative potential of biological molecules. Produced as soluble monomers, they assemble into multimeric membrane-inserted complexes in response to specific membrane environments. Actinoporins, a class of pore-forming proteins from sea anemones, target membranes to kill cells. Here, we report cryogenic electron microscopy structures of two actinoporins, fragaceatoxin C and sticholysin II, reconstituted in lipid membranes. The structures reveal an ordered arrangement of dozens of lipid molecules that form an integral part of the pore architecture. We also captured distinct oligomeric intermediates, arc-shaped assemblies with monomers in transitional conformations, representing key snapshots along the pore formation pathway. These data provide direct structural evidence for a stepwise mechanism in which monomers sequentially bind the membrane and undergo conformational changes that drive pore assembly and membrane disruption. Our findings reveal how these proteins reshape membranes and offer mechanistic insights into their cytolytic activity. This work broadens our understanding of pore-forming proteins, which are gaining increasing relevance in diverse biotechnological applications.
External linksSci Adv / PubMed:40991702 / PubMed Central
MethodsEM (single particle)
Resolution2.1 - 4.9 Å
Structure data

51384

9gj8

EMDB-51384, PDB-9gj8:
Structure of Sticholisin II in large unilamellar vesicles.
Method: EM (single particle) / Resolution: 2.1 Å

51420

9gki

EMDB-51420, PDB-9gki:
Structure of 5mer pore intermediate of Sticholysin II (StnII) toxin in lipid nanodiscs
Method: EM (single particle) / Resolution: 3.8 Å

51426

9gkl

EMDB-51426, PDB-9gkl:
Structure of the octameric pore of Fragaceotxin C (FraC or DELTA-actitoxin-Afr1a) in large unilamellar vesicles.
Method: EM (single particle) / Resolution: 2.5 Å

51431

9gko

EMDB-51431, PDB-9gko:
Structure of 6mer pore intermediate of Sticholysin II (StnII) toxin in lipid nanodiscs
Method: EM (single particle) / Resolution: 4.9 Å

51432

9gkp

EMDB-51432, PDB-9gkp:
Structure of fragacetoxin C in lipid nanodiscs
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-FO4:
sphingomyelin

ChemComp-CLR:
CHOLESTEROL

ChemComp-HOH:
WATER

Source
  • stichodactyla helianthus (sea anemone)
  • actinia fragacea (sea anemone)
KeywordsMEMBRANE PROTEIN / sticholisin / nanodisc / toxin / actinoporin / LUVs

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