› 4ep5

X-ray diffraction
2.08Å resolution

Thermus thermophilus RuvC structure

Released:
DOI: 10.2210/pdb4ep5/pdb
PDB entry 4ep5 coloured by chain, front view.
PDB entry 4ep5 coloured by chain, side view.
PDB entry 4ep5 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution.
Chen L, Shi K, Yin Z, Aihara H
Nucleic Acids Res 41 648-56 (2013)
PMID: 23118486

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178012 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Crossover junction endodeoxyribonuclease RuvC Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 17.78 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SJC4 (Residues: 1-166; Coverage: 100%)
Gene names: TTHA1090, ruvC
Sequence domains: Crossover junction endodeoxyribonuclease RuvC
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I212121
Unit cell:
a: 35.183Å b: 60.019Å c: 135.734Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.208 0.261
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Holliday junction resolvases.
Wyatt et al. (2014)
1 more

5 mentions without citation

Hijacked then lost in translation: the plight of the recombinant host cell in membrane protein structural biology projects.
Bill et al. (2015)
4 more