9EYN

The structure of solubilized octameric pore of actinoporin Fav prepared on DOPC, cholesterol, sphingomyelin membranes

これはPDB形式変換不可エントリーです。

9EYN の概要

• エントリーDOI: 10.2210/pdb9eyn/pdb
• 関連するPDBエントリー: 9EYL 9EYM 9EYO
• EMDBエントリー: 50058 50060
• 分子名称: Actinoporin, CHOLESTEROL, Sphingomyelin C18 (3 entities in total)
• 機能のキーワード: actinoporin, pore-forming toxin, pore, octamer, transmembrane pore, toxin, cholesterol, nanopore
• 由来する生物種: Orbicella faveolata
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 295509.42

構造登録者

Solinc, G.,Srnko, M.,Svigel, T.,Anderluh, G.,Podobnik, M. (登録日: 2024-04-09, 公開日: 2025-04-23, 最終更新日: 2025-11-05)

主引用文献

Solinc, G.,Srnko, M.,Merzel, F.,Crnkovic, A.,Kozorog, M.,Podobnik, M.,Anderluh, G.
Cryo-EM structures of a protein pore reveal a cluster of cholesterol molecules and diverse roles of membrane lipids.
Nat Commun, 16:2972-2972, 2025

PubMed Abstract: The structure and function of membrane proteins depend on their interactions with lipids that constitute membranes. Actinoporins are α-pore-forming proteins that bind preferentially to sphingomyelin-containing membranes, where they oligomerize and form transmembrane pores. Through a comprehensive cryo-electron microscopic analysis of a pore formed by an actinoporin Fav from the coral Orbicella faveolata, we show that the octameric pore interacts with 112 lipids in the upper leaflet of the membrane, reveal the roles of lipids, and demonstrate that the actinoporin surface is suited for binding multiple receptor sphingomyelin molecules. When cholesterol is present in the membrane, it forms a cluster of four molecules associated with each protomer. Atomistic simulations support the structural data and reveal additional effects of the pore on the lipid membrane. These data reveal a complex network of protein-lipid and lipid-lipid interactions and an underrated role of lipids in the structure and function of transmembrane protein complexes.

PubMed: 40140423
DOI: 10.1038/s41467-025-58334-z

実験手法

ELECTRON MICROSCOPY (3.06 Å)