File:Toxins-02-01612-g001.png

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British English: Crystal structure of cholera toxin. The heterodimeric CTA protein subunit (blue) is composed of two polypeptide chains, CTA1 (22 kDa) and CTA2 (5 kDa), linked by a single disulfide bond. The enzymatically active CTA1 peptide is the (toxic) mono-ADP-ribosyltransferase subunit, while the CTA2 helical peptide links the CTA1 subunit to the pentameric CTB subunits. The cholera toxin B subunit (10.6 kDa) is composed of five identical polypeptide subunit chains (yellow, purple, red, orange, and turquoise), each with membrane receptor GM1ganglioside binding capacity.
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Source Fig. 1 at https://www.mdpi.com/2072-6651/2/7/1612/htm AB Toxins: A Paradigm Switch from Deadly to Desirable. In: MDPI Toxins 2010, 2(7), Special Issue Enterotoxins, pp1612-1645; doi:10.3390/toxins2071612
Author Oludare Odumosu, Dequina Nicholas, Hiroshi Yano, William Langridge
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