<unk>  from Bordetella pertussis is a 1706 amino acid residue long protein. The protein consists of three domains: from the N-terminus up to roughly residue 400, there is an<unk><unk>  domain; between residues 500 and 700, there is a hydrophobic domain; and from residue 1000 to the C-terminus, there are calcium binding repeats. Two acylation sites are located at lysine residues K860 and K983. The part of the toxin from residue 400 to the C-terminus, called hemolysin, is structurally related to a large family of bacterial toxins - RTX toxins. Differences between the toxins of different Bordetella species are mainly in the calcium-binding domain. Folding and secretion The toxin is secreted by the Type I secretion system, which spans both membranes and periplasm space, allowing the toxin to be secreted from the cytoplasm straight outside the cell. A large proportion of the toxin remains associated with the bacterium exterior proteins, mainly filamentous haemagglutinin, but these toxin molecules are not<unk> ive. Besides attachment to bacterial proteins, aggregation also inactivates the toxin. This quick inactivation highlights the necessity of close contact between secreting bacterium and target cell.
Adenylate cyclase toxin
Grammotoxin
Chlorotoxin
Vanillotoxin
Cyanotoxin
Neurotoxin
Alpha-neurotoxin
Diamphotoxin