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Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

Degiacomi, Matteo T. and Iacovache, Ioan and Pernot, Lucile and Chami, Mohamed and Kudryashev, Misha and Stahlberg, Henning and van der Goot, F. Gisou and Dal Peraro, Matteo. (2013) Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. Nature chemical biology, Vol. 9, H. 10. pp. 623-629.

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Official URL: http://edoc.unibas.ch/dok/A6183900

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Abstract

Aerolysin is the founding member of a superfamily of β-pore-forming toxins whose pore structure is unknown. We have combined X-ray crystallography, cryo-EM, molecular dynamics and computational modeling to determine the structures of aerolysin mutants in their monomeric and heptameric forms, trapped at various stages of the pore formation process. A dynamic modeling approach based on swarm intelligence was applied, whereby the intrinsic flexibility of aerolysin extracted from new X-ray structures was used to fully exploit the cryo-EM spatial restraints. Using this integrated strategy, we obtained a radically new arrangement of the prepore conformation and a near-atomistic structure of the aerolysin pore, which is fully consistent with all of the biochemical data available so far. Upon transition from the prepore to pore, the aerolysin heptamer shows a unique concerted swirling movement, accompanied by a vertical collapse of the complex, ultimately leading to the insertion of a transmembrane β-barrel.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:1552-4450
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:06 Dec 2013 09:35
Deposited On:06 Dec 2013 09:35

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