3LIM
Crystal structure of the pore forming toxin frac from sea anemone actinia fragacea
3LIM の概要
| エントリーDOI | 10.2210/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: 21300287DOI: 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) |
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