Structure of a Cholesterol-Binding, Thiol-Activated Cytolysin and a Model of Its Membrane Form

1997/05/01 by Jamie Rossjohn, Susanne C. Feil, Susanne C Feil +6 · 15 citations
Biochemistry, Genetics and Molecular Biology · Immunology and Microbiology · #Calcium signaling and nucleotide metabolism #Lipid Membrane Structure and Behavior #Toxin Mechanisms and Immunotoxins

paper · pdf · doi:10.1016/s0092-8674(00)80251-2

crossref issued 1997/05/01 · crossref published 1997/05/01 · crossref published-print 1997/05/01 · openalex publication_date 1997/05/01 · crossref created 2004/05/04 · crossref deposited 2021/06/17 · openalex created_date 2025/10/10 · crossref indexed 2026/06/27 · openalex updated_date 2026/07/22

Citations

• PROCHECK: a program to check the stereochemical quality of protein structures
• Effect of lipidic factors on membrane cholesterol topology — mode of binding of θ-toxin to cholesterol in liposomes

Cited by

• Vertical collapse of a cytolysin prepore moves its transmembrane β‐hairpins to the membrane
• Structure of the Lectin Regulatory Domain of the Cholesterol-Dependent Cytolysin Lectinolysin Reveals the Basis for Its Lewis Antigen Specificity
• Cholesterol Exposure at the Membrane Surface Is Necessary and Sufficient to Trigger Perfringolysin O Binding
• Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy
• The Cholesterol-Dependent Cytolysin Signature Motif: A Critical Element in the Allosteric Pathway that Couples Membrane Binding to Pore Assembly
• Molecular basis of listeriolysin O pH dependence
• The Mechanism of Membrane Insertion for a Cholesterol-Dependent Cytolysin
• Arresting Pore Formation of a Cholesterol-dependent Cytolysin by Disulfide Trapping Synchronizes the Insertion of the Transmembrane β-Sheet from a Prepore Intermediate
• Monomer-Monomer Interactions Drive the Prepore to Pore Conversion of a β-Barrel-forming Cholesterol-dependent Cytolysin
• Monomer-Monomer Interactions Propagate Structural Transitions Necessary for Pore Formation by the Cholesterol-dependent Cytolysins
• Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
• Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand alignment
• The Cholesterol-Dependent Cytolysin Family of Gram-Positive Bacterial Toxins
• Differential interaction of the two cholesterol‐dependent, membrane‐damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol
• Cholesterol-dependent cytolysin [wikipedia]