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Cholera toxin
From Proteopedia
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[[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]. | ||
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Revision as of 01:12, 4 May 2012
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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].
3D Structures of Cholera toxin
Updated November 2011
CTX
1xtc - CTX
CTX A subunit
2a5d, 2a5g – CTX A subunit+hArf6+GTP – human
2a5f - CTX A subunit+hArf6+GTP+NAD
1s5b, 1s5c, 1s5d, 1s5e, 1s5f - CTX A subunit (mutant)
CTX B subunits
1fgb - CTX B subunits
1g8z , 1chp, 1chq - CTX B subunits (mutant)
1rcv, 1rd9, 1rdp, 1rf2, 1pzi, 1pzj, 1pzk, 1efi, 1eef, 1djr, 1eei – CTX B subunits+ galactoside derivatives
1llr, 1jqy, 1jr0, 1fd7, 1md2 - CTX B subunits+BMSC derivatives
1eef - CTX B subunits+PEPG
3chb, 2chb - CTX B subunits+pentasaccharide
1ct1 - CTX B subunits (mutant)+pentasaccharide
3efx – CTX B/heat-labile enterotoxin B chain
1tet – CTX peptide 3+FAB light and heavy chains - mouse
