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Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins.
Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.
Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin.
Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane.
Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins.
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Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins.
Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins. J Mol Biol. 2007 Apr 13; 367(5):1227-36.
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PubMed
subject areas
Bacterial Toxins
Cholesterol
Crystallography, X-Ray
Dimerization
Hemolysin Proteins
Hydrogen-Ion Concentration
Membrane Glycoproteins
Models, Molecular
Perforin
Pore Forming Cytotoxic Proteins
Protein Structure, Tertiary
Rotation
Tryptophan
authors with profiles
Rodney Kim Tweten