1s5c: Difference between revisions
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{{STRUCTURE_1s5c| PDB=1s5c | SCENE= }} | |||
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'''Cholera holotoxin with an A-subunit Y30S mutation, Crystal form 1''' | '''Cholera holotoxin with an A-subunit Y30S mutation, Crystal form 1''' | ||
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==Reference== | ==Reference== | ||
Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism., O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG, Biochemistry. 2004 Apr 6;43(13):3772-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15049684 15049684] | Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism., O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG, Biochemistry. 2004 Apr 6;43(13):3772-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15049684 15049684] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
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[[Category: Jobling, M G.]] | [[Category: Jobling, M G.]] | ||
[[Category: Neal, C J.O.]] | [[Category: Neal, C J.O.]] | ||
[[Category: | [[Category: Ab5 toxin]] | ||
[[Category: | [[Category: Adp ribose transferase]] | ||
[[Category: | [[Category: Cholera toxin]] | ||
[[Category: | [[Category: Heat-labile enterotoxin]] | ||
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Revision as of 08:19, 3 May 2008
Cholera holotoxin with an A-subunit Y30S mutation, Crystal form 1
OverviewOverview
Cholera toxin (CT) is a heterohexameric bacterial protein toxin belonging to a larger family of A/B ADP-ribosylating toxins. Each of these toxins undergoes limited proteolysis and/or disulfide bond reduction to form the enzymatically active toxic fragment. Nicking and reduction render both CT and the closely related heat-labile enterotoxin from Escherichia coli (LT) unstable in solution, thus far preventing a full structural understanding of the conformational changes resulting from toxin activation. We present the first structural glimpse of an active CT in structures from three crystal forms of a single-site A-subunit CT variant, Y30S, which requires no activational modifications for full activity. We also redetermined the structure of the wild-type, proenzyme CT from two crystal forms, both of which exhibit (i) better geometry and (ii) a different A2 "tail" conformation than the previously determined structure [Zhang et al. (1995) J. Mol. Biol. 251, 563-573]. Differences between wild-type CT and active CTY30S are observed in A-subunit loop regions that had been previously implicated in activation by analysis of the structure of an LT A-subunit R7K variant [van den Akker et al. (1995) Biochemistry 34, 10996-11004]. The 25-36 activation loop is disordered in CTY30S, while the 47-56 active site loop displays varying degrees of order in the three CTY30S structures, suggesting that disorder in the activation loop predisposes the active site loop to a greater degree of flexibility than that found in unactivated wild-type CT. On the basis of these six new views of the CT holotoxin, we propose a model for how the activational modifications experienced by wild-type CT are communicated to the active site.
About this StructureAbout this Structure
1S5C is a Protein complex structure of sequences from Vibrio cholerae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism., O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG, Biochemistry. 2004 Apr 6;43(13):3772-82. PMID:15049684 Page seeded by OCA on Sat May 3 08:19:13 2008