Sandbox Reserved 496
From Proteopedia
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'''Cholix Toxin''' named also CT, is a protein toxin that uses ADP-ribosyltransferases to modify target proteins in human cells. The mono-ADP-ribosyltransferase toxins are bacterial virulence factors that are believed to be a factor in many disease states in animals plants as well even humans. For a list of various and other similar toxins see [[Toxins]]. | '''Cholix Toxin''' named also CT, is a protein toxin that uses ADP-ribosyltransferases to modify target proteins in human cells. The mono-ADP-ribosyltransferase toxins are bacterial virulence factors that are believed to be a factor in many disease states in animals plants as well even humans. For a list of various and other similar toxins see [[Toxins]]. | ||
- | <Structure load=' | + | <Structure load='569B' size='300' color='white' frame='true' align='right' caption='testcaption' /> |
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== Cholix Toxin from ''Vibrio Cholerae ''== | == Cholix Toxin from ''Vibrio Cholerae ''== | ||
- | The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of the [http://en.wikipedia.org/wiki/Proteolysis proteolytically] activated monomeric form of Cyt2Ba was determined at | + | The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of the [http://en.wikipedia.org/wiki/Proteolysis proteolytically] activated monomeric form of Cyt2Ba was determined at 2.1Å resolution. It consists of a single domain of <scene name='Cyt2Ba/Alpha_beta/5'>α/β</scene> architecture with a <scene name='Cyt2Ba/Beta/2'>β-sheet</scene> (yellow) surrounded by 2 <scene name='Cyt2Ba/Alpha/2'>α-helical</scene> layers <font color='red'><b>(red)</b></font> forming a cytolysin fold. |
Revision as of 20:01, 29 April 2012
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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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Cholix Toxin from Vibrio CholeraeThe crystal structure of the proteolytically activated monomeric form of Cyt2Ba was determined at 2.1Å resolution. It consists of a single domain of architecture with a (yellow) surrounded by 2 layers (red) forming a cytolysin fold. |