› 1q57

X-ray diffraction
3.45Å resolution

The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7

Released:
DOI: 10.2210/pdb1q57/pdb
PDB entry 1q57 coloured by chain, front view.
PDB entry 1q57 coloured by chain, side view.
PDB entry 1q57 coloured by chain, top view.
Source organism: Escherichia phage T7
Primary publication:
The crystal structure of the bifunctional primase-helicase of bacteriophage T7.
Toth EA, Li Y, Sawaya MR, Cheng Y, Ellenberger T
Mol Cell 12 1113-23 (2003)
PMID: 14636571

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137203 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA helicase/primase Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 503 amino acids
Theoretical weight: 55.86 KDa
Source organism: Escherichia phage T7
Expression system: Escherichia coli
UniProt:
  • Canonical: P03692 (Residues: 64-566; Coverage: 89%)
Gene name: 4
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 117.179Å b: 171.567Å c: 118.581Å
α: 90° β: 99.86° γ: 90°
R-values:
R R work R free
0.301 0.299 0.326
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Structure and mechanism of helicases and nucleic acid translocases.
Singleton et al. (2007)
21 more

14 mentions without citation

Understanding helicases as a means of virus control.
Frick et al. (2006)
13 more