› 5jzt

Electron Microscopy
7.4Å resolution

Cryo-EM structure of aerolysin pore in LMNG micelle

Released:
DOI: 10.2210/pdb5jzt/pdb
PDB entry 5jzt coloured by chain, front view.
PDB entry 5jzt coloured by chain, side view.
PDB entry 5jzt 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-8187

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aerolysin Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 424 amino acids
Theoretical weight: 47.19 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: 7.4Å
Relevant EMDB volumes: EMD-8187
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

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

19 mentions without citation

Molecular mechanism of pore formation by aerolysin-like proteins.
Podobnik et al. (2017)
18 more