2hof

X-ray diffraction
2.4Å resolution

Crystal structure of the pre-cleavage synaptic complex in the cre-loxp site-specific recombination

Released:
Source organism: Escherichia virus P1
Primary publication:
Synapsis of loxP sites by Cre recombinase.
J Biol Chem 282 24004-16 (2007)
PMID: 17573343

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Recombinase cre Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 38.54 KDa
Source organism: Escherichia virus P1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06956 (Residues: 1-343; Coverage: 100%)
Gene name: cre
Sequence domains: Phage integrase family
Structure domains:
LoxP DNA Chain: C
Molecule details ›
Chain: C
Length: 35 nucleotides
Theoretical weight: 10.7 KDa
Source organism: Escherichia virus P1
Expression system: Not provided
LoxP DNA Chain: D
Molecule details ›
Chain: D
Length: 35 nucleotides
Theoretical weight: 10.82 KDa
Source organism: Escherichia virus P1
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2221
Unit cell:
a: 107.625Å b: 122.13Å c: 178.748Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.209 0.263
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided