2q5t
From Proteopedia
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| - | [[Image:2q5t.jpg|left|200px]] | + | [[Image:2q5t.jpg|left|200px]] |
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| - | '''Full-length Cholix toxin from Vibrio Cholerae''' | + | {{Structure |
| + | |PDB= 2q5t |SIZE=350|CAPTION= <scene name='initialview01'>2q5t</scene>, resolution 2.10Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Residue+A+801'>AC1</scene>, <scene name='pdbsite=AC2:Edo+Binding+Site+For+Residue+A+900'>AC2</scene>, <scene name='pdbsite=AC3:Edo+Binding+Site+For+Residue+A+901'>AC3</scene>, <scene name='pdbsite=AC4:Edo+Binding+Site+For+Residue+A+902'>AC4</scene>, <scene name='pdbsite=AC5:Edo+Binding+Site+For+Residue+A+903'>AC5</scene>, <scene name='pdbsite=AC6:Edo+Binding+Site+For+Residue+A+904'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+A+905'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+A+906'>AC8</scene> and <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+A+907'>AC9</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae]) | ||
| + | }} | ||
| + | |||
| + | '''Full-length Cholix toxin from Vibrio Cholerae''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2Q5T is a [ | + | 2Q5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q5T OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18276581 18276581] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:22:05 2008'' |
Revision as of 16:22, 20 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , and | ||||||
| Ligands: | and | ||||||
| Gene: | toxA (Vibrio cholerae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Full-length Cholix toxin from Vibrio Cholerae
Overview
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.
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 Thu Mar 20 18:22:05 2008
