PDBsum entry 3c0m

Toxin

PDB id: 3c0m

Contents

Protein chains

449 a.a. *

Waters ×24

* Residue conservation analysis

PDB id:

3c0m

Name:

Toxin

Title:

Crystal structure of the proaerolysin mutant y221g

Structure:

Aerolysin. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Aeromonas hydrophila. Organism_taxid: 644. Gene: aera. Expressed in: aeromonas salmonicida. Expression_system_taxid: 645.

Resolution:

2.88Å R-factor: 0.199 R-free: 0.252

Authors:

L.Pernot,M.Schiltz,S.Thurnheer,S.E.Burr,G.Van Der Goot

Key ref:

M.T.Degiacomi et al. (2013). Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. Nat Chem Biol, 9, 623-629. PubMed id: 23912165 DOI: 10.1038/nchembio.1312

Date:

21-Jan-08 Release date: 12-Feb-08

Protein chains

P09167  (AERA_AERHY) -  Aerolysin from Aeromonas hydrophila

Seq: 493 a.a.

Struc: 449 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/nchembio.1312

Nat Chem Biol 9:623-629 (2013)

PubMed id: 23912165

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

M.T.Degiacomi, I.Iacovache, L.Pernot, M.Chami, M.Kudryashev, H.Stahlberg, F.G.van der Goot, M.Dal Peraro.

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.