2Q5T
Full-length Cholix toxin from Vibrio Cholerae
Summary for 2Q5T
| Entry DOI | 10.2210/pdb2q5t/pdb |
| Descriptor | Cholix toxin, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | domain i (receptor binding domain), beta barrel, domain ii (translocation domain), six alpha-helix bundle, domain iii (catalytic domain), alpha-beta complex, toxin |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 1 |
| Total formula weight | 72502.50 |
| Authors | Jorgensen, R.,Fieldhouse, R.J.,Merrill, A.R. (deposition date: 2007-06-01, release date: 2008-02-12, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 18276581DOI: 10.1074/jbc.M710008200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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