3C0N

Crystal structure of the proaerolysin mutant Y221G at 2.2 A

Summary for 3C0N

• Entry DOI: 10.2210/pdb3c0n/pdb
• Related: 1PRE 3C0M 3C0O
• Descriptor: Aerolysin (2 entities in total)
• Functional Keywords: toxin, cytolytic toxin, pore-forming toxin
• Biological source: Aeromonas hydrophila
• Cellular location: Secreted: P09167
• Total number of polymer chains: 2
• Total formula weight: 103748.66

Authors

Pernot, L.,Schiltz, M.,Thurnheer, S.,Burr, S.E.,van der Goot, G. (deposition date: 2008-01-21, release date: 2008-02-12, Last modification date: 2024-10-30)

Primary citation

Degiacomi, M.T.,Iacovache, I.,Pernot, L.,Chami, M.,Kudryashev, M.,Stahlberg, H.,van der Goot, F.G.,Dal Peraro, M.
Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism.
Nat.Chem.Biol., 9:623-629, 2013

PubMed 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.

PubMed: 23912165
DOI: 10.1038/nchembio.1312

Experimental method

X-RAY DIFFRACTION (2.2 Å)