3iuo

X-ray diffraction
1.6Å resolution

The Crystal Structure of the C-terminal domain of the ATP-dependent DNA helicase RecQ from Porphyromonas gingivalis to 1.6A

Released:
Source organism: Porphyromonas gingivalis
Entry authors: Stein AJ, Sather A, Duggan E, Moy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
PDBe Complex ID:
PDB-CPX-181773 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent DNA helicase RecQ Chains: A, B
Molecule details ›
Chains: A, B
Length: 122 amino acids
Theoretical weight: 14.53 KDa
Source organism: Porphyromonas gingivalis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7MX11 (Residues: 604-725; Coverage: 17%)
Gene names: PG_0416, recQ-1
Sequence domains: RecQ-1-like, helix-turn-helix domain
Structure domains: ATP-dependent DNA helicase RecQ

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R3
Unit cell:
a: 98.326Å b: 98.326Å c: 72.526Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.221
Expression system: Escherichia coli BL21(DE3)