Capturing the Membrane-Triggered Conformational Transition of an α‑Helical Pore-Forming Toxin

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 thi...

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Veröffentlicht in:	The journal of physical chemistry. B 2016-12, Vol.120 (47), p.12064-12078
Hauptverfasser:	Giri Rao, V. V. Hemanth, Desikan, Rajat, Ayappa, K. Ganapathy, Gosavi, Shachi
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Cell Membrane - chemistry Cell Membrane - metabolism Escherichia coli - chemistry Escherichia coli - metabolism Escherichia coli - pathogenicity Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Hemolysin Proteins - chemistry Hemolysin Proteins - metabolism Hydrophobic and Hydrophilic Interactions Kinetics Molecular Dynamics Simulation Pore Forming Cytotoxic Proteins - chemistry Pore Forming Cytotoxic Proteins - metabolism Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Solubility Thermodynamics
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