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| - | [[Image:2q5t.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2q5t| PDB=2q5t | SCENE= }} | | {{STRUCTURE_2q5t| PDB=2q5t | SCENE= }} |
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| - | '''Full-length Cholix toxin from Vibrio Cholerae'''
| + | ===Full-length Cholix toxin from Vibrio Cholerae=== |
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| - | ==Overview==
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| - | 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<SUB>50</SUB> = 4.6 +/- 0.4 ng/mL) and crustaceans (Artemia nauplii LD<SUB>50</SUB> = 10 +/- 2 microg/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 multi-domain 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 ADPRT 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_18276581}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18276581 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18276581}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Six alpha-helix bundle]] | | [[Category: Six alpha-helix bundle]] |
| | [[Category: Toxin]] | | [[Category: Toxin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:31:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:36:51 2008'' |
Revision as of 06:36, 29 July 2008
Template:STRUCTURE 2q5t
Full-length Cholix toxin from Vibrio Cholerae
Template:ABSTRACT PUBMED 18276581
About this Structure
2Q5T is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
Reference
Cholix toxin, a novel ADP-ribosylating factor from vibrio cholerae., Jorgensen R, Purdy AE, Fieldhouse RJ, Kimber MS, Bartlett DH, Rod Merrill A, J Biol Chem. 2008 Feb 25;. PMID:18276581
Page seeded by OCA on Tue Jul 29 09:36:51 2008
