Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins.
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Summary
Crystal structures of PFO are presented that reveal a detailed molecular pathway that may be the basis for the allosteric transition that occurs on initial membrane binding leading to the exposure of membrane-spanning regions in a domain distant from the initial site of interaction.
- Type
- review
- Published
- 2007-04-13
- Cited by
- 95
- References
- 47
- Access
- Open access
- OpenAlex
- https://openalex.org/W1990554391
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12277845
Keywords
Allosteric regulation, Membrane, Biophysics, Chemistry, Transmembrane protein
References
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- The comprehensive sourcebook of bacterial protein toxins
- Processing of X-ray diffraction data collected in oscillation mode.
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- Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells
- Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us.
- Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.
- Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins.
- Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
- An efficient routine for computing symmetric real spherical harmonics for high orders of expansion
- PROCHECK: a program to check the stereochemical quality of protein structures
- Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation.
- Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae.
- Crystallography & NMR system: A new software suite for macromolecular structure determination.
- A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
- Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy.
- The CCP4 suite: programs for protein crystallography.
- The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation.
- The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins.
Cited by
- Cholesterol-protein interaction: methods and cholesterol reporter molecules.
- Perfringolysin O: The Underrated Clostridium perfringens Toxin?
- Role of membrane lipids for the activity of pore forming peptides and proteins.
- Identification and Characterization of Inerolysin, the Cholesterol Dependent Cytolysin produced by Lactobacillus iners
- Cholesterol-dependent cytolysins.
- Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins.
- Vibrio cholerae cytolysin: structure-function mechanism of an atypical β-barrel pore-forming toxin.
- Fluorescence imaging of MACPF/CDC proteins: new techniques and their application.
- Engineering Probes to Detect Cholesterol Accessibility on Membranes Using Perfringolysin O
- pH dependence of listeriolysin O aggregation and pore‐forming ability
- Toxins from Bacteria
- Development of a Single-Gene, Signature-Tag-Based Approach in Combination with Alanine Mutagenesis To Identify Listeriolysin O Residues Critical for the In Vivo Survival of Listeria monocytogenes
- Pore formation: an ancient yet complex form of attack.
- Cholesterol microcrystals and cochleate cylinders: attachment of pyolysin oligomers and domain 4.
- A New Model for Pore Formation by Cholesterol-Dependent Cytolysins
- Bacterial Toxins and the Nervous System: Neurotoxins and Multipotential Toxins Interacting with Neuronal Cells
- Obstructing toxin pathways by targeted pore blockage
- Structure of Human C8 Protein Provides Mechanistic Insight into Membrane Pore Formation by Complement*
- Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59
- Structure of Human Complement C8, a Precursor to Membrane Attack
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