› 3gud

X-ray diffraction
2.2Å resolution

Crystal structure of a novel intramolecular chaperon

Released:
DOI: 10.2210/pdb3gud/pdb
PDB entry 3gud coloured by chain, front view.
PDB entry 3gud coloured by chain, side view.
PDB entry 3gud coloured by chain, top view.
Source organism: Bacillus virus GA1
Primary publication:
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.
Schulz EC, Dickmanns A, Urlaub H, Schmitt A, Mühlenhoff M, Stummeyer K, Schwarzer D, Gerardy-Schahn R, Ficner R
Nat Struct Mol Biol 17 210-5 (2010)
PMID: 20118935

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S74 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 15.24 KDa
Source organism: Bacillus virus GA1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FZW3 (Residues: 620-740; Coverage: 16%)
Gene name: gene 12
Sequence domains: Chaperone of endosialidase
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

4 bound ligands:
Ligand BR 1 x BR
Ligand PEG 1 x PEG
Ligand CL 1 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3
Unit cell:
a: 84.04Å b: 84.04Å c: 41.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.197 0.232
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Knitting and snipping: chaperones in β-helix folding.
Schulz et al. (2011)
1 more

10 mentions without citation

Bacteriophage protein-protein interactions.
Häuser et al. (2012)
9 more