Cholera toxin: Difference between revisions

Yang Yang (talk | contribs)
No edit summary
Yang Yang (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1xtc.png|left|200px|thumb|Crystal Structure of Cholera toxin [[1xtc]]]]
[[Image:1xtc.png|left|200px|thumb|Crystal Structure of Cholera toxin [[1xtc]]]]
{{STRUCTURE_1xtc|  PDB=1xtc  | SIZE=300| SCENE=Cholera_toxin/Cv/1 |right|CAPTION=Cholera toxin [[1xtc]] }}
{{STRUCTURE_1xtc|  PDB=1xtc  | SIZE=300| SCENE=Cholera_toxin/Cv/1 |right|CAPTION=Cholera toxin [[1xtc]] }}
Cholera toxin (CTX), a protein complex released by Vibrio cholerae, has two types of subunits: subunit A and subunit B. A subunit contains A1 domain, which includes the enzymatic active site, and A2 domain, which has a α–helix tail. The B subunit contains five chains that form a pentameric ring around the central pore in structure; Subunit A and subunit B are assembled by the α–helix tail of A2 domain, which inserts into the central pore. CTX the main virulence factor of the pathogen Vibrio cholerae and cause the major symptom of infection: extreme diarrhea, vomiting, cramps and even death [1][2][3].


[[Cholera toxin]] (CTX) from the bacterium ''Vibrio cholerae'' is an oligomeric complex of an enzymatic subunit (chain A) and 5 copies of chain B which bind to the cell surface.  The enzymatic subunit has a globular domain (CTA1) and a long helical domain (CTA2).  Once the CTX binds to the cell surface, it is internalized, and its CTA1 domain binds to ADP-ribosylation factor 6 (Arf6) enabling its catalytic activity. The images at the left and at the right correspond to the crystal structure of cholera toxin ([[1xtc]]).  For toxins in Proteopedia see [[Toxins]].
[[Cholera toxin]] (CTX) from the bacterium ''Vibrio cholerae'' is an oligomeric complex of an enzymatic subunit (chain A) and 5 copies of chain B which bind to the cell surface.  The enzymatic subunit has a globular domain (CTA1) and a long helical domain (CTA2).  Once the CTX binds to the cell surface, it is internalized, and its CTA1 domain binds to ADP-ribosylation factor 6 (Arf6) enabling its catalytic activity. The images at the left and at the right correspond to the crystal structure of cholera toxin ([[1xtc]]).  For toxins in Proteopedia see [[Toxins]].
Cholera toxin (CTX), a protein complex released by Vibrio cholerae, has two types of subunits: subunit A and subunit B. A subunit contains A1 domain, which includes the enzymatic active site, and A2 domain, which has a α–helix tail. The B subunit contains five chains that form a pentameric ring around the central pore in structure; Subunit A and subunit B are assembled by the α–helix tail of A2 domain, which inserts into the central pore. CTX the main virulence factor of the pathogen Vibrio cholerae and cause the major symptom of infection: extreme diarrhea, vomiting, cramps and even death [1][2][3].
 
 


{{TOC limit|limit=2}}
{{TOC limit|limit=2}}

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Yang Yang