2BK2	Cytolytic Protein	date	Feb 08, 2005
title	The Prepore 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 Microscopy	resolution	28.00 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	Chain Function Process Component A cholesterol binding pathogenesis
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

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (18 Kb) [Save to disk] Biological Unit Coordinates (2bk2.pdb1.gz) 300 Kb CSU: Contacts of Structural Units for 2BK2 Likely Quarternary Molecular Structure file(s) for 2BK2 Retrieve 2BK2 in mmCIF format [Save to disk]

View 2BK2 in 3D

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 2BK2, from MSDmotif at EBI Fold representative 2bk2 from FSSP and Dali (Families of Structurally Similar Proteins)

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [2bk2_A]

Other resources with information on 2BK2

InterPro: IPR001869 MMDB (Entrez's Structure Database)

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