› 5gaq

Electron Microscopy
3.14Å resolution

Cryo-EM structure of the Lysenin Pore

Released:
DOI: 10.2210/pdb5gaq/pdb
PDB entry 5gaq coloured by chain, front view.
PDB entry 5gaq coloured by chain, side view.
PDB entry 5gaq coloured by chain, top view.
Source organism: Eisenia fetida
Primary publication:
Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.
Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, Savva CG
Nat Commun 7 11293 (2016)
PMID: 27048994
Related structures: EMD-8015

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysenin Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 310 amino acids
Theoretical weight: 34.98 KDa
Source organism: Eisenia fetida
Expression system: Escherichia coli
UniProt:
  • Canonical: O18423 (Residues: 1-297; Coverage: 100%)
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.14Å
Relevant EMDB volumes: EMD-8015
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Electron Cryo-microscopy as a Tool for Structure-Based Drug Development.
Merino et al. (2017)
15 more

9 mentions without citation

Structural Basis of the Pore-Forming Toxin/Membrane Interaction.
Li et al. (2021)
8 more