2Q5T

Full-length Cholix toxin from Vibrio Cholerae

2Q5T の概要

• エントリーDOI: 10.2210/pdb2q5t/pdb
• 分子名称: Cholix toxin, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: domain i (receptor binding domain), beta barrel, domain ii (translocation domain), six alpha-helix bundle, domain iii (catalytic domain), alpha-beta complex, toxin
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 72502.50

構造登録者

Jorgensen, R.,Fieldhouse, R.J.,Merrill, A.R. (登録日: 2007-06-01, 公開日: 2008-02-12, 最終更新日: 2024-10-30)

主引用文献

Jorgensen, R.,Purdy, A.E.,Fieldhouse, R.J.,Kimber, M.S.,Bartlett, D.H.,Merrill, A.R.
Cholix Toxin, a Novel ADP-ribosylating Factor from Vibrio cholerae.
J.Biol.Chem., 283:10671-10678, 2008

PubMed Abstract: The ADP-ribosyltransferases are a class of enzymes that display activity in a variety of bacterial pathogens responsible for causing diseases in plants and animals, including those affecting mankind, such as diphtheria, cholera, and whooping cough. We report the characterization of a novel toxin from Vibrio cholerae, which we call cholix toxin. The toxin is active against mammalian cells (IC(50) = 4.6 +/- 0.4 ng/ml) and crustaceans (Artemia nauplii LD(50) = 10 +/- 2 mug/ml). Here we show that this toxin is the third member of the diphthamide-specific class of ADP-ribose transferases and that it possesses specific ADP-ribose transferase activity against ribosomal eukaryotic elongation factor 2. We also describe the high resolution crystal structures of the multidomain toxin and its catalytic domain at 2.1- and 1.25-A resolution, respectively. The new structural data show that cholix toxin possesses the necessary molecular features required for infection of eukaryotes by receptor-mediated endocytosis, translocation to the host cytoplasm, and inhibition of protein synthesis by specific modification of elongation factor 2. The crystal structures also provide important insight into the structural basis for activation of toxin ADP-ribosyltransferase activity. These results indicate that cholix toxin may be an important virulence factor of Vibrio cholerae that likely plays a significant role in the survival of the organism in an aquatic environment.

PubMed: 18276581
DOI: 10.1074/jbc.M710008200

実験手法

X-RAY DIFFRACTION (2.1 Å)