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3LIM

Crystal structure of the pore forming toxin frac from sea anemone actinia fragacea

3LIM の概要
エントリーDOI10.2210/pdb3lim/pdb
分子名称Fragaceatoxin C, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
機能のキーワードpore forming toxin, actinoporins, toxin
由来する生物種Actinia fragacea (sea anemones)
細胞内の位置Secreted (By similarity): B9W5G6
タンパク質・核酸の鎖数6
化学式量合計122084.59
構造登録者
Mechaly, A.E.,Bellomio, A.,Morante, K.,Gonzalez-Manas, J.M.,Guerin, D.M.A. (登録日: 2010-01-25, 公開日: 2010-12-15, 最終更新日: 2024-02-21)
主引用文献Mechaly, A.E.,Bellomio, A.,Gil-Carton, D.,Morante, K.,Valle, M.,Gonzalez-Manas, J.M.,Guerin, D.M.
Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins.
Structure, 19:181-191, 2011
Cited by
PubMed Abstract: Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 Å resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free α-helical bundle pore.
PubMed: 21300287
DOI: 10.1016/j.str.2010.11.013
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 3lim
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-08に公開中

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