Cholera toxin: Difference between revisions
No edit summary |
No edit summary |
||
| Line 9: | Line 9: | ||
== Structure == | == Structure == | ||
Cholera toxin(CTX) 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) 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]. | ||
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]]). The images at the lower left correspond to the assumed biological molecule structure ([[]]) toxins in Proteopedia see [[Toxins]]. | 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]]). The images at the lower left correspond to the assumed biological molecule structure ([[1xtc]]) toxins in Proteopedia see [[Toxins]]. | ||
| Line 48: | Line 48: | ||
[[3efx]] – CTX B/heat-labile enterotoxin B chain<br /> | [[3efx]] – CTX B/heat-labile enterotoxin B chain<br /> | ||
[[1tet]] – CTX peptide 3+FAB light and heavy chains - mouse | [[1tet]] – CTX peptide 3+FAB light and heavy chains - mouse | ||
== Reference == | |||
[1] Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology (4th ed.). McGraw Hill. p. 375. ISBN 0838585299. | |||
[2] Faruque SM; Nair GB (editors). (2008). Vibrio cholerae: Genomics and Molecular Biology. Caister Academic Press. ISBN 978-1-904455-33-2 . | |||
[3] Jennifer McDowall, Cholera Toxin, EMBL-EMI, Interpro | |||
[4] Davis B, Waldor M (2003). "Filamentous phages linked to virulence of Vibrio cholerae". Curr Opin Microbiol 6 (1): 35–42. doi:10.1016/S1369-5274(02)00005-X. PMID 12615217. | |||
[5] Pierre-Hervé Luppi. "The Discovery of Cholera-Toxin as a Powerful Neuroanatomical Tool". Retrieved 2011-03-23. | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||