2BK1 | Cytolytic Protein | date | Feb 10, 2005 ![]() ![]() |
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title | The Pore Structure Of Pneumolysin, Obtained By Fitting The Alpha Carbon Trace Of Perfringolysin O Into A Cryo-Em Map | ||||||||||||||
authors | S.J.Tilley, E.V.Orlova, R.J.C.Gilbert, P.W.Andrew, H.R.Saibil | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Perfringolysin O Chain: A Engineered: Yes |
Organism_scientific: Clostridium Perfringens Expression_system: Escherichia Coli | ||||||||||||||
symmetry | Space Group: P 1 | R_factor | |||||||||||||
crystal cell |
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method | Cryo-Electron Microscopy | resolution | 29.00 Å | ||||||||||||
similarity | Belongs to the thiol-activated cytolysin family.[Thiol_cytolysin] | ||||||||||||||
subunit | Forms oligomers in the host membrane. | ||||||||||||||
Genes | CPE0163, PFOA, PFOR, PFO (C. perfringens) | ||||||||||||||
function | Cholesterol is the receptor for the binding of these toxins to eukaryotic cell membranes. Is able to lyse cholesterol containing membranes. Sulfhydryl-activated toxin. Can be reversibly inactivated by oxidation. | ||||||||||||||
Gene Ontology |
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Primary reference | Structural basis of pore formation by the bacterial toxin pneumolysin., Tilley SJ, Orlova EV, Gilbert RJ, Andrew PW, Saibil HR, Cell. 2005 Apr 22;121(2):247-56. PMID:15851031 |
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