Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy

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DOIResolve DOI: http://doi.org/10.1021/bi00487a017
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TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume29
Issue35
Pages81068111
AbstractThe structure and thermal stability of isolated B and A subunits of cholera toxin, as well as the interaction of the B subunit with a ganglioside GM₁ receptor, were studied by Fourier-transform infrared spectroscopy. the B subunit of the toxin is highly folded; its secondary structure consists predominantly of β-sheets. The temperature dependence of the infrared spectrum indicates that the B subunit undergoes thermal unfolding in the temperature range between approximately 66 and 78 ºC. Binding to the ganglioside GM₁ receptor or to its oligosaccharide moiety results in only marginal, if any, change in the secondary structure of the B subunit; however, the receptor-associated subunit does show a markedly increased thermal stability. The secondary structure of the enzymatically active A subunit is less ordered and much less stable than that of the B subunit. The relatively loose folding of the A subunit is likely to be of importance for the effective membrane translocation of this subunit.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NRC number30582
NPARC number23001498
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Record identifiere9107a78-46e0-4428-a48d-511c22ec8f73
Record created2017-02-20
Record modified2017-02-20
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