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1PRE

PROAEROLYSIN

1PRE の概要
エントリーDOI10.2210/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: 7510043
DOI: 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)
構造検証レポート
Validation report summary of 1pre
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2026-03-04に公開中

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