Clostridium botulinum C3 toxin

Action

The molecular basis of the action of these enzymes consists in binding of nicotinamide adenine dinucleotide (NAD), splitting NAD into its ADP-ribose and nicotinamide components, and transferring the ADP-ribose moiety to a specific residue on to a protein substrate, often of eukaryotic origin. All the toxins of this family share a highly conserved glutamate, which is the catalytic residue critical for the NAD-glycohydrolase activity. ADP-ribosyltransferase toxins have distinct substrate specificities and variable pathophysiological properties and can be subdivided into four subfamilies: diphtheria-like toxins, cholera-like toxins, binary toxins and C3-like exoenzymes.

C3-like exoenzymes unlike other ADP-ribosyltransferase toxins do not require a specific cell-surface binding translocation component for cell entry. Their specificity is for the small GTP-binding proteins RhoA, RhoB, and RhoC, which are ADP-ribosylated on an asparagine residue.

References

1. (May 2008). "Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes". Protein Science.
2. (1990). "ADP-ribosylating Toxins and G Protein, Insights into Signal Transduction". American Society for Microbiology.