› 5ly6

Electron Microscopy
4.5Å resolution

CryoEM structure of the membrane pore complex of Pneumolysin at 4.5A

Released:
DOI: 10.2210/pdb5ly6/pdb
PDB entry 5ly6 coloured by chain, front view.
PDB entry 5ly6 coloured by chain, side view.
PDB entry 5ly6 coloured by chain, top view.
Source organism: Streptococcus pneumoniae D39
Primary publication:
CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.
van Pee K, Neuhaus A, D'Imprima E, Mills DJ, Kühlbrandt W, Yildiz Ö
OpenAccess logo Elife 6 (2017)
PMID: 28323617
Related structures: EMD-4118

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pneumolysin Chain: B
Molecule details ›
Chain: B
Length: 471 amino acids
Theoretical weight: 52.87 KDa
Source organism: Streptococcus pneumoniae D39
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q04IN8 (Residues: 1-471; Coverage: 100%)
Gene names: SPD_1726, ply
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.5Å
Relevant EMDB volumes: EMD-4118
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

The gasdermins, a protein family executing cell death and inflammation.
Broz et al. (2020)
13 more

14 mentions without citation

Cholesterol-dependent cytolysins: from water-soluble state to membrane pore.
Christie et al. (2018)
13 more