CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin

CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin

Many pathogenic bacteria produce pore-forming toxins to attack and kill human cells. We have determined the 4.5 Å structure of the ~2.2 MDa pore complex of pneumolysin, the main virulence factor of Streptococcus pneumoniae, by cryoEM. The pneumolysin pore is a 400 Å ring of 42 membrane-inserted mono...

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Bibliographic Details
Main Authors: Katharina van Pee, Alexander Neuhaus, Edoardo D'Imprima, Deryck J Mills, Werner Kühlbrandt, Özkan Yildiz
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2017-03-01
Series:eLife
Subjects:
cholesterol-dependent cytolysin (CDC)
membrane pore
pore-forming toxin
electron cryo-microscopy (cryoEM)
electron cryo-tomography (cryoET)
X-ray crystallography
Online Access:https://elifesciences.org/articles/23644

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https://elifesciences.org/articles/23644

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