1hh1

X-ray diffraction
2.15Å resolution

THE STRUCTURE OF HJC, A HOLLIDAY JUNCTION RESOLVING ENZYME FROM SULFOLOBUS SOLFATARICUS

Released:
Source organism: Saccharolobus solfataricus
Primary publication:
Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricus.
Proc Natl Acad Sci U S A 98 5509-14 (2001)
PMID: 11331763

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-181673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Crossover junction endodeoxyribonuclease Hjc Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16.04 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7LXU0 (Residues: 1-143; Coverage: 100%)
Gene names: ORF-c21_024, SSO0575, hjc
Sequence domains: Archaeal holliday junction resolvase (hjc)
Structure domains: Trna Endonuclease; Chain: A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P6122
Unit cell:
a: 52.699Å b: 52.699Å c: 207.607Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.22 0.281
Expression system: Escherichia coli