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PDBsum entry 3c0m

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Toxin PDB id
3c0m
Contents
Protein chains
449 a.a.
Waters ×24

References listed in PDB file
Key reference
Title Molecular assembly of the aerolysin pore reveals a swirling membrane-Insertion mechanism.
Authors M.T.Degiacomi, I.Iacovache, L.Pernot, M.Chami, M.Kudryashev, H.Stahlberg, F.G.Van der goot, M.Dal peraro.
Ref. Nat Chem Biol, 2013, 9, 623-629. [DOI no: 10.1038/nchembio.1312]
PubMed id 23912165
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.
Secondary reference #1
Title Structure of the aeromonas toxin proaerolysin in its water-Soluble and membrane-Channel states.
Authors M.W.Parker, J.T.Buckley, J.P.Postma, A.D.Tucker, K.Leonard, F.Pattus, D.Tsernoglou.
Ref. Nature, 1994, 367, 292-295.
PubMed id 7510043
Abstract
Secondary reference #2
Title Crystallization of a proform of aerolysin, A hole-Forming toxin from aeromonas hydrophila.
Authors A.D.Tucker, M.W.Parker, D.Tsernoglou, J.T.Buckley.
Ref. J Mol Biol, 1990, 212, 561-562.
PubMed id 2329576
Abstract
PROCHECK
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