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- W2543120616 abstract "Escherichia coli cytolysin A (ClyA) is an α-helical pore-forming toxin (PFT) which lyses target cells by forming membrane permeabilizing pores. The rate-determining step of this process is the conversion of the soluble ClyA monomer into a membrane inserted protomer. We elucidate the mechanism of this conformational transition using molecular dynamics simulations of coarse-grained models of ClyA and a membrane. We find that a membrane is necessary for the conformational conversion because membrane–protein interactions counteract the loss of the many intraprotein hydrophobic interactions that stabilize the membrane-inserting segments in the ClyA monomer. Of the two membrane-inserting segments, the flexible and highly hydrophobic β-tongue inserts first while the insertion of helix αA1 is membrane assisted. We conclude that the β-tongue is designed to behave as a quick-response membrane sensor, while helix αA1 improves target selectivity for cholesterol-containing cell membranes by acting as a fidelity check." @default.
- W2543120616 created "2016-11-04" @default.
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- W2543120616 date "2016-11-17" @default.
- W2543120616 modified "2023-10-10" @default.
- W2543120616 title "Capturing the Membrane-Triggered Conformational Transition of an α-Helical Pore-Forming Toxin" @default.
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- W2543120616 doi "https://doi.org/10.1021/acs.jpcb.6b09400" @default.
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- W2543120616 hasPublicationYear "2016" @default.
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