期刊
NATURE CHEMICAL BIOLOGY
卷 9, 期 10, 页码 623-629出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1312
关键词
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资金
- Swiss National Science Foundation [200021_122120, 200020_138013]
- Swiss Initiative for Systems Biology, SystemsX.ch
- Swiss National Science Foundation (SNF) [200021_122120, 200020_138013] Funding Source: Swiss National Science Foundation (SNF)
Aerolysin is the founding member of a superfamily of (beta-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 beta-barrel.
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