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• W2018054206 abstract "FRET measurements were used to determine the domain-specific topography of perfringolysin O, a pore-forming toxin, on a membrane surface at different stages of pore formation. The data reveal that the elongated toxin monomer binds stably to the membrane in an “end-on” orientation, with its long axis approximately perpendicular to the plane of the membrane bilayer. This orientation is largely retained even after monomer association to form an oligomeric prepore complex. The domain 3 (D3) polypeptide segments that ultimately form transmembrane β-hairpins remain far above the membrane surface in both the membrane-bound monomer and prepore oligomer. Upon pore formation, these segments enter the bilayer, whereas D1 moves to a position that is substantially closer to the membrane. Therefore, the extended D2 β-structure that connects D1 to membrane-bound D4 appears to bend or otherwise reconfigure during the prepore-to-pore transition of the perfringolysin O oligomer." @default.
• W2018054206 created "2016-06-24" @default.
• W2018054206 creator A5001106575 @default.
• W2018054206 creator A5032321673 @default.
• W2018054206 creator A5044088516 @default.
• W2018054206 date "2005-05-06" @default.
• W2018054206 modified "2023-10-01" @default.
• W2018054206 title "The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation" @default.
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• W2018054206 doi "https://doi.org/10.1073/pnas.0500556102" @default.
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