9GKL

Structure of the octameric pore of Fragaceotxin C (FraC or DELTA-actitoxin-Afr1a) in large unilamellar vesicles.

9GKL の概要

• エントリーDOI: 10.2210/pdb9gkl/pdb
• 関連するPDBエントリー: 9GJ8 9GKI 9GKO 9GKP
• EMDBエントリー: 51384 51420 51426 51431 51432
• 分子名称: DELTA-actitoxin-Afr1a, sphingomyelin, CHOLESTEROL, ... (4 entities in total)
• 機能のキーワード: membrane protein, luvs, nanodisc, toxin, actinoporin
• 由来する生物種: Actinia fragacea
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 228271.50

構造登録者

Martin Benito, J.,Santiago, C.,Carlero, D.,Arranz, R. (登録日: 2024-08-25, 公開日: 2025-10-08, 最終更新日: 2025-10-29)

主引用文献

Arranz, R.,Santiago, C.,Masiulis, S.,Rivera-de-Torre, E.,Palacios-Ortega, J.,Carlero, D.,Heras-Marquez, D.,Gavilanes, J.G.,Arias-Palomo, E.,Martinez-Del-Pozo, A.,Garcia-Linares, S.,Martin-Benito, J.
Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.
Sci Adv, 11:eadv0683-eadv0683, 2025

PubMed Abstract: 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.

PubMed: 40991702
DOI: 10.1126/sciadv.adv0683

実験手法

ELECTRON MICROSCOPY (2.5 Å)