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

MPG-Autoren
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van Pee,  Katharina
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Neuhaus,  Alexander
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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D'Imprima,  Edoardo
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Mills,  Deryck J.       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Yildiz,  Özkan       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

van Pee, K., Neuhaus, A., D'Imprima, E., Mills, D. J., Kühlbrandt, W., & Yildiz, Ö. (2017). CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin. eLife, 6: e23644. doi:10.7554/eLife.23644.001.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002D-4853-9
Zusammenfassung
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 monomers. Domain 3 of the soluble toxin refolds into two ~85 Å β-hairpins that traverse the lipid bilayer and assemble into a 168-strand β-barrel. The pore complex is stabilized by salt bridges between β-hairpins of adjacent subunits and an internal α-barrel. The apolar outer barrel surface with large sidechains is immersed in the lipid bilayer, while the inner barrel surface is highly charged. Comparison of the cryoEM pore complex to the prepore structure obtained by electron cryo-tomography and the x-ray structure of the soluble form reveals the detailed mechanisms by which the toxin monomers insert into the lipid bilayer to perforate the target membrane.