Structural Basis of the Pore-Forming Toxin/Membrane Interaction
نویسندگان
چکیده
منابع مشابه
Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59
Pore-forming proteins containing the structurally conserved membrane attack complex/perforin fold play an important role in immunity and host-pathogen interactions. Intermedilysin (ILY) is an archetypal member of a cholesterol-dependent cytolysin subclass that hijacks the complement receptor CD59 to make cytotoxic pores in human cells. ILY directly competes for the membrane attack complex bindi...
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Soluble oligomers are potent toxins in many neurodegenerative diseases, but little is known about the structure of soluble oligomers and their structure-toxicity relationship. Here we prepared onpathway oligomers of the 140-residue protein R-synuclein, a key player in Parkinson’s disease, at concentrations an order of magnitude higher than previously possible. The oligomers form ion channels wi...
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The human pathogen Streptococcus pneumoniae produces soluble pneumolysin monomers that bind host cell membranes to form ring-shaped, oligomeric pores. We have determined three-dimensional structures of a helical oligomer of pneumolysin and of a membrane-bound ring form by cryo-electron microscopy. Fitting the four domains from the crystal structure of the closely related perfringolysin reveals ...
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The bacterial toxin pneumolysin is released as a soluble monomer that kills target cells by assembling into large oligomeric rings and forming pores in cholesterol-containing membranes. Using cryo-EM and image processing, we have determined the structures of membrane-surface bound (prepore) and inserted-pore oligomer forms, providing a direct observation of the conformational transition into th...
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ژورنال
عنوان ژورنال: Toxins
سال: 2021
ISSN: 2072-6651
DOI: 10.3390/toxins13020128