Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins.
The recently determined structures of three different protein toxins by X-ray crystallography has unexpectedly revealed a common membrane-insertion domain. This domain consists of an alpha-helical bundle of between seven and ten helices, some of which are hydrophobic. The three toxins, colicin, insecticidal delta-endotoxin and diphtheria toxin are directed towards different hosts, have different killing mechanisms and bear no sequence homology. The observation of a common membrane-insertion domain has implications for the design of therapeutic agents in combating disease.
Parker
M W
MW
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
Pattus
F
F
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry*; D001427:Bacterial Toxins; D003087:Colicins / Q000737:chemistry*; D004167:Diphtheria Toxin / Q000737:chemistry*; D004731:Endotoxins / Q000737:chemistry*; D006460:Hemolysin Proteins; D008565:Membrane Proteins / Q000737:chemistry; D011487:Protein Conformation; D012995:Solubility; D014867:Water
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D003087:Colicins; D004167:Diphtheria Toxin; D004731:Endotoxins; D006460:Hemolysin Proteins; D008565:Membrane Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D014867:Water