1gm5

X-ray diffraction
3.24Å resolution

Structure of RecG bound to three-way DNA junction

Released:
Source organism: Thermotoga maritima
Primary publication:
Structural analysis of DNA replication fork reversal by RecG.
Cell 107 79-89 (2001)
PMID: 11595187

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
3 distinct DNA molecules
Macromolecules (4 distinct):
ATP-dependent DNA helicase RecG Chain: A
Molecule details ›
Chain: A
Length: 780 amino acids
Theoretical weight: 90.06 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WY48 (Residues: 1-780; Coverage: 100%)
Gene names: TM_0205, recG
Sequence domains:
Structure domains:
DNA (5'-(*CP*AP*GP*CP*TP*CP*CP*AP*TP*GP*AP*TP* CP*AP*TP*TP*GP*GP*CP*A)-3') Chain: X
Molecule details ›
Chain: X
Length: 20 nucleotides
Theoretical weight: 6.09 KDa
Source organism: Thermotoga maritima
Expression system: Not provided
DNA (5'-(*GP*CP*AP*GP*TP*GP*CP*TP*CP*GP*CP*AP* TP*GP*GP*AP*GP*CP*TP*G)-3') Chain: Y
Molecule details ›
Chain: Y
Length: 20 nucleotides
Theoretical weight: 6.19 KDa
Source organism: Thermotoga maritima
Expression system: Not provided
DNA (5'-(*GP*AP*GP*CP*AP*CP*TP*GP*C)-3') Chain: Z
Molecule details ›
Chain: Z
Length: 9 nucleotides
Theoretical weight: 2.74 KDa
Source organism: Thermotoga maritima
Expression system: Not provided

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 133.704Å b: 144.602Å c: 84.023Å
α: 90° β: 113.82° γ: 90°
R-values:
R R work R free
0.275 0.272 0.328
Expression systems:
  • Escherichia coli
  • Not provided