4TSN

Crystal structure of FraC with POC bound (crystal form II)

4TSN の概要

• エントリーDOI: 10.2210/pdb4tsn/pdb
• 関連するPDBエントリー: 3VWI 3W9P 4TSL 4TSO 4TSP 4TSQ 4TSY
• 分子名称: Fragaceatoxin C, PHOSPHOCHOLINE, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: toxin, actinoporin, pore-forming toxin, membrane lipids, phosphocholine, lipid-protein interaction
• 由来する生物種: Actinia fragacea (Strawberry anemone)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 81821.36

構造登録者

Caaveiro, J.M.M.,Tanaka, K.,Tsumoto, K. (登録日: 2014-06-19, 公開日: 2015-03-04, 最終更新日: 2023-11-08)

主引用文献

Tanaka, K.,Caaveiro, J.M.M.,Morante, K.,Gonzalez-Manas, J.M.,Tsumoto, K.
Structural basis for self-assembly of a cytolytic pore lined by protein and lipid
Nat Commun, 6:6337-6337, 2015

PubMed Abstract: Pore-forming toxins (PFT) are water-soluble proteins that possess the remarkable ability to self-assemble on the membrane of target cells, where they form pores causing cell damage. Here, we elucidate the mechanism of action of the haemolytic protein fragaceatoxin C (FraC), a α-barrel PFT, by determining the crystal structures of FraC at four different stages of the lytic mechanism, namely the water-soluble state, the monomeric lipid-bound form, an assembly intermediate and the fully assembled transmembrane pore. The structure of the transmembrane pore exhibits a unique architecture composed of both protein and lipids, with some of the lipids lining the pore wall, acting as assembly cofactors. The pore also exhibits lateral fenestrations that expose the hydrophobic core of the membrane to the aqueous environment. The incorporation of lipids from the target membrane within the structure of the pore provides a membrane-specific trigger for the activation of a haemolytic toxin.

PubMed: 25716479
DOI: 10.1038/ncomms7337

実験手法

X-RAY DIFFRACTION (1.57 Å)