› 5jzw

Electron Microscopy
4.46Å resolution

Cryo-EM structures of aerolysin post-prepore and quasipore

Released:
DOI: 10.2210/pdb5jzw/pdb
PDB entry 5jzw coloured by chain, front view.
PDB entry 5jzw coloured by chain, side view.
PDB entry 5jzw coloured by chain, top view.
Source organism: Aeromonas hydrophila
Primary publication:
Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.
Iacovache I, De Carlo S, Cirauqui N, Dal Peraro M, van der Goot FG, Zuber B
Nat Commun 7 12062 (2016)
PMID: 27405240
Related structures: EMD-8188

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140579 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aerolysin Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 424 amino acids
Theoretical weight: 47.13 KDa
Source organism: Aeromonas hydrophila
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09167 (Residues: 24-447; Coverage: 90%)
Gene name: aerA
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.46Å
Relevant EMDB volumes: EMD-8188
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

Targeting and alteration of tight junctions by bacteria and their virulence factors such as Clostridium perfringens enterotoxin.
Eichner et al. (2017)
18 more

4 mentions without citation

Advances in cryoEM and its impact on β-pore forming proteins.
Boyd et al. (2018)
3 more