2BK1 Cytolytic Protein date Feb 10, 2005
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
length a length b length c angle alpha angle beta angle gamma
1.000 1.000 1.000 90.00 90.00 90.00
method Cryo-Electron Microscopyresolution 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
ChainFunctionProcessComponent
A
  • lipid binding
  • cholesterol binding
  • pathogenesis
  • cytolysis
  • hemolysis by symbiont of hos...

  • Primary referenceStructural 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
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (18 Kb) [Save to disk]
  • Biological Unit Coordinates (2bk1.pdb1.gz) 353 Kb
  • CSU: Contacts of Structural Units for 2BK1
  • Likely Quarternary Molecular Structure file(s) for 2BK1
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  • View one-letter amino acid or nucleotide sequence for each chain: [2bk1_A]
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  • InterPro: IPR001869
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