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Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.
Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment.
Disulfide-bond scanning reveals assembly state and ß-strand tilt angle of the PFO ß-barrel.
The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins.
Assembly and topography of the prepore complex in cholesterol-dependent cytolysins.
Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane.
The Cholesterol-dependent Cytolysin Membrane-binding Interface Discriminates Lipid Environments of Cholesterol to Support ß-Barrel Pore Insertion.
Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin.
The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae.
Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.