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1DM0

SHIGA TOXIN

1DM0 の概要
エントリーDOI10.2210/pdb1dm0/pdb
分子名称SHIGA TOXIN A SUBUNIT, SHIGA TOXIN B SUBUNIT (3 entities in total)
機能のキーワードab5 structure, polypeptide a, blocking, active site, toxin
由来する生物種Shigella dysenteriae
詳細
タンパク質・核酸の鎖数12
化学式量合計140109.61
構造登録者
Fraser, M.E.,Chernaia, M.M.,Kozlov, Y.V.,James, M.N. (登録日: 1999-12-13, 公開日: 1999-12-30, 最終更新日: 2024-10-16)
主引用文献Fraser, M.E.,Chernaia, M.M.,Kozlov, Y.V.,James, M.N.
Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution.
Nat.Struct.Biol., 1:59-64, 1994
Cited by
PubMed Abstract: Shigella dysenteriae is the pathogen responsible for the severe form of dysentery in humans. It produces Shiga toxin, the prototype of a family of closely related bacterial protein toxins. We have determined the structure of the holotoxin, an AB5 hexamer, by X-ray crystallography. The five B subunits form a pentameric ring, encircling a helix at the carboxy terminus of the A subunit. The A subunit interacts with the B pentamer via this C-terminal helix and a four-stranded mixed beta-sheet. The fold of the rest of the A subunit is similar to that of the A chain of the plant toxin ricin; both are N-glycosidases. However, the active site in the bacterial holotoxin is blocked by a segment of polypeptide chain. These residues of the A subunit would be released as part of the activation mechanism of the toxin.
PubMed: 7656009
DOI: 10.1038/nsb0194-59
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1dm0
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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