Taxonomic distribution of proteins containing Aerolysin domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Aerolysin domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Structure of the Aeromonas toxin proaerolysin in its water-soluble andmembrane-channel states.

Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D
Nature. 1994; 367: 292-5

Aerolysin is chiefly responsible for the pathogenicity of Aeromonashydrophila, a bacterium associated with diarrhoeal diseases and deep woundinfections. Like many other microbial toxins, the protein changes in amultistep process from a completely water-soluble form to produce atransmembrane channel that destroys sensitive cells by breaking theirpermeability barriers. Here we describe the structure of proaerolysindetermined by X-ray crystallography at 2.8 A resolution. The protoxin(M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomerderived from electron microscopy have assisted in constructing a model ofthe membrane channel and have led to the proposal of a scheme to accountfor insertion of the protein into lipid bilayers to form ion channels.

Nucleotide sequence of the gene for the hole-forming toxin aerolysin ofAeromonas hydrophila.

Howard SP, Garland WJ, Green MJ, Buckley JT
J Bacteriol. 1987; 169: 2869-71

The gene for the hole-forming toxin aerolysin from Aeromonas hydrophilawas sequenced. Although most of the sequence seems unrelated to that ofStaphylococcus aureus alpha-toxin, both proteins are very hydrophilic, andthey each contain a nearly identical string of 10 amino acids.