Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin.
Epsilon-toxin from Clostridium perfringens is a lethal toxin. Recent studies suggest that the toxin acts via an unusually potent pore-forming mechanism. Here we report the crystal structure of epsilon-toxin, which reveals structural similarity to aerolysin from Aeromonas hydrophila. Pore-forming toxins can change conformation between soluble and transmembrane states. By comparing the two toxins, we have identified regions important for this transformation.
Cole
Ambrose R
AR
Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, UK.
Gibert
Maryse
M
Popoff
Michel
M
Moss
David S
DS
Titball
Richard W
RW
Basak
Ajit K
AK
D000333:Aeromonas / Q000378:metabolism; D000595:Amino Acid Sequence; D001407:Bacillus / Q000378:metabolism; D001427:Bacterial Toxins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D052899:Pore Forming Cytotoxic Proteins; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D001427:Bacterial Toxins; C039811:Clostridium perfringens epsilon-toxin; D052899:Pore Forming Cytotoxic Proteins; C032676:aerolysin