Sandbox Reserved 481
From Proteopedia
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== Structure == | == Structure == | ||
| - | To observe the structure, the Cholix Toxin was crystallized by vapor diffusion against reservoirs containing 23% polyethlene gylcol-10,000, 7.5% ethylene glycol, and 0.1 m HERPES. In addition, the reservoirs were at a pH 7.5 and at a temperature of 19°C. | + | To observe the structure, the Cholix Toxin was crystallized by vapor diffusion against reservoirs containing 23% polyethlene gylcol-10,000, 7.5% ethylene glycol, and 0.1 m HERPES. In addition, the reservoirs were kept at a of pH 7.5 and at a temperature of 19°C. About 40 µL of reservior solution containg 1.25 mM NAD+ solution was added to a 2 µL crystal containg droup. The NAD+ was allowed to soak into the crystals for approximately 2-3 minutes. The crystals were then transffered to paratone-N for visualization. |
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| + | Cholix Toxin contains three different domains. Domain I is the receptor binding domain containing two beta sheets. Domain II is the translocation domain. It is considered a multi-helical domain that is able to unfold within the membrane. | ||
<Structure load='2q5t' size='400' frame='true' align='right' caption='Protein Structure of Cholix Toxin' scene='Insert optional scene name here' /> | <Structure load='2q5t' size='400' frame='true' align='right' caption='Protein Structure of Cholix Toxin' scene='Insert optional scene name here' /> | ||
Revision as of 07:24, 1 May 2012
| This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500. | |||||||
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IntroductionCholix toxin (CT) are a class of protein toxin originating from the bacteria Vibrio Cholerae. The toxin uses ADP-riboyltransferase to inactivate eukaryotic elongation factor 2 by transferring ADP-ribose from NAD+ which inhibits protein synthesis and causes cell death. This protein toxin has been known to cause disease in both plants and animals. Specifically, the toxin can cause the disease Cholera. It enters eukaryotic cells through cell mediated endocytosis. Once inside, the toxin transfers an ADP-ribose group to an Arg residue of the GTP binding protein G. This then activates adenylate cyclase which leads to an increase amount of cAMP, causing a secretion of Cl-,HCO3-, and water from epithelial cells from the site of colonization. The result is dehydration and loss of electrolytes in mammals. Cholix toxins are composed of a receptor binding, translocation, and catalytic domain. StructureTo observe the structure, the Cholix Toxin was crystallized by vapor diffusion against reservoirs containing 23% polyethlene gylcol-10,000, 7.5% ethylene glycol, and 0.1 m HERPES. In addition, the reservoirs were kept at a of pH 7.5 and at a temperature of 19°C. About 40 µL of reservior solution containg 1.25 mM NAD+ solution was added to a 2 µL crystal containg droup. The NAD+ was allowed to soak into the crystals for approximately 2-3 minutes. The crystals were then transffered to paratone-N for visualization. Cholix Toxin contains three different domains. Domain I is the receptor binding domain containing two beta sheets. Domain II is the translocation domain. It is considered a multi-helical domain that is able to unfold within the membrane.
Mechanism of ActionMedical Implications or Possible ApplicationsReferences1. The 1.8A Cholix Toxin Crystal Structure in Complex with NAD+ and Evidence for a New Kinetic Model |
