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

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.

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van Pee, Katharina1, Autor           
Neuhaus, Alexander1, Autor           
D'Imprima, Edoardo1, Autor           
Mills, Deryck J.1, Autor                 
Kühlbrandt, Werner1, Autor                 
Yildiz, Özkan1, Autor                 
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Schlagwörter: X-ray crystallography; biophysics; cholesterol-dependent cytolysin (CDC); electron cryo-microscopy (cryoEM); electron cryo-tomography (cryoET); infectious disease; membrane pore; microbiology; pore-forming toxin; structural biology
 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.

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Sprache(n): eng - English
 Datum: 20172016-11-282017-03-172017-03-21
 Publikationsstatus: Online veröffentlicht
 Seiten: 22
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.7554/eLife.23644.001
 Art des Abschluß: -

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Titel: eLife
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Cambridge : eLife Sciences Publications
Seiten: - Band / Heft: 6 Artikelnummer: e23644 Start- / Endseite: - Identifikator: Anderer: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X