1BCP

BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP

1BCP の概要

• エントリーDOI: 10.2210/pdb1bcp/pdb
• 分子名称: PERTUSSIS TOXIN, ADENOSINE-5'-TRIPHOSPHATE, ... (7 entities in total)
• 機能のキーワード: toxin, adp-ribosyltransferase, transferase, whooping cough
• 由来する生物種: Bordetella pertussis; 詳細
• 細胞内の位置: Secreted: P04977 P04978 P04979 P0A3R5 P04981
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 211371.73

構造登録者

Hazes, B.,Read, R.J. (登録日: 1995-11-21, 公開日: 1997-06-05, 最終更新日: 2024-11-06)

主引用文献

Hazes, B.,Boodhoo, A.,Cockle, S.A.,Read, R.J.
Crystal structure of the pertussis toxin-ATP complex: a molecular sensor.
J.Mol.Biol., 258:661-671, 1996

PubMed Abstract: Pertussis toxin is a major virulence factor of Bordetella pertussis, the causative agent of whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). In vitro experiments have shown that ATP and a number of detergents and phospholipids assist in activating the holotoxin by destabilizing the interaction between S1 and the B-oligomer. Similar processes may play a role in the activation of pertussis toxin in vivo. In this paper we present the crystal structure of the pertussis toxin-ATP complex and discuss the structural basis for the ATP-induced activation. In addition, we propose a physiological role for the ATP effect in the process by which the toxin enters the cytoplasm of eukaryotic cells. The key features of this proposal are that ATP binding signals the arrival of the toxin in the endoplasmic reticulum and, at the same time, triggers dissociation of the holotoxin prior to membrane translocation.

PubMed: 8637000
DOI: 10.1006/jmbi.1996.0277

実験手法

X-RAY DIFFRACTION (2.7 Å)