Structural basis of pore formation by cholesterol-binding toxins.
In this paper we describe reconstructions by electron cryo-microscopy of two oligomeric states of the pore-forming toxin pneumolysin. The results are interpreted by the fitting of atomic models of separated domains to the 3-dimensional electron density maps, revealing two steps in the mechanism of pore formation by the family of cholesterol-binding toxins. We briefly describe the observation of the toxin pore in model membranes and contrast the apparent mechanism of pneumolysin with that of other pore-forming toxins.
Gilbert
R J
RJ
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, Oxford, UK. gilbert@strbi.ox.ac.uk
Jiménez
J L
JL
Chen
S
S
Andrew
P W
PW
Saibil
H R
HR
D001426:Bacterial Proteins; D001427:Bacterial Toxins / Q000737:chemistry; D002784:Cholesterol / Q000378:metabolism*; D003603:Cytotoxins / Q000737:chemistry*; D006460:Hemolysin Proteins; D008854:Microscopy, Electron; D011487:Protein Conformation; D021122:Protein Subunits; D013301:Streptolysins / Q000737:chemistry*
D001426:Bacterial Proteins; D001427:Bacterial Toxins; D003603:Cytotoxins; D006460:Hemolysin Proteins; D021122:Protein Subunits; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae; C020452:Clostridium perfringens theta-toxin; D002784:Cholesterol