› 1ty2

X-ray diffraction
2Å resolution

Crystal structure of the streptococcal pyrogenic exotoxin J (SPE-J)

Released:
DOI: 10.2210/pdb1ty2/pdb
PDB 1ty2 coloured by chain and viewed from the front.
PDB 1ty2 coloured by chain and viewed from the side.
PDB 1ty2 coloured by chain and viewed from the top.
Source organism: Streptococcus pyogenes
Primary publication:
Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization.
Baker HM, Proft T, Webb PD, Arcus VL, Fraser JD, Baker EN
J Biol Chem 279 38571-6 (2004)
PMID: 15247241

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exotoxin J Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 211 amino acids
Theoretical weight: 24.8 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7BAE3 (Residues: 22-232; Coverage: 91%)
Gene name: speJ
Sequence domains: Staphylococcal/Streptococcal toxin, beta-grasp domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 167.33Å b: 46.33Å c: 72.22Å
α: 90° β: 90.54° γ: 90°
R-values:
R R work R free
0.231 0.218 0.249
Expression system: Escherichia coli

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Citations

1 review citation

Streptococcus pyogenes: Insight into the function of the streptococcal superantigens.
Sriskandan et al. (2007)
4 other articles