1PRE
PROAEROLYSIN
1PRE の概要
| エントリーDOI | 10.2210/pdb1pre/pdb |
| 分子名称 | PROAEROLYSIN (2 entities in total) |
| 機能のキーワード | toxin (hemolytic polypeptide) |
| 由来する生物種 | Aeromonas hydrophila |
| 細胞内の位置 | Secreted: P09167 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 103960.91 |
| 構造登録者 | Parker, M.W.,Buckley, J.T.,Postma, J.P.M.,Tucker, A.D.,Tsernoglou, D. (登録日: 1995-09-15, 公開日: 1996-10-14, 最終更新日: 2024-10-16) |
| 主引用文献 | Parker, M.W.,Buckley, J.T.,Postma, J.P.,Tucker, A.D.,Leonard, K.,Pattus, F.,Tsernoglou, D. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature, 367:292-295, 1994 Cited by PubMed Abstract: Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 A resolution. The protoxin (M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels. PubMed: 7510043DOI: 10.1038/367292a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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