› 4kyp

X-ray diffraction
1.7Å resolution

Beta-Scorpion Toxin folded in the periplasm of E.coli

Released:
DOI: 10.2210/pdb4kyp/pdb
PDB entry 4kyp coloured by chain, front view.
PDB entry 4kyp coloured by chain, side view.
PDB entry 4kyp coloured by chain, top view.
Source organism: Hottentotta judaicus
Primary publication:
Chaperone-mediated native folding of a ��-scorpion toxin in the periplasm of Escherichia coli.
O'Reilly AO, Cole AR, Lopes JL, Lampert A, Wallace BA
Biochim. Biophys. Acta 1840 10-5 (2014)
PMID: 23999087

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-157507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-insect excitatory toxin Bj-xtrIT Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 84 amino acids
Theoretical weight: 9.44 KDa
Source organism: Hottentotta judaicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P56637 (Residues: 19-94; Coverage: 100%)
Sequence domains: Scorpion toxin-like domain
Structure domains: Knottin, scorpion toxin-like

Ligands and Environments

2 bound ligands:
Ligand PGE 2 x PGE
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2221
Unit cell:
a: 41.87Å b: 88.56Å c: 183.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.229
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Microbial production of toxins from the scorpion venom: properties and applications.
Amorim et al. (2018)
7 other articles

1 mention without citation

Chaperone-mediated native folding of a β-scorpion toxin in the periplasm of Escherichia coli.
O'Reilly et al. (2014)