2biw

X-ray diffraction
2.39Å resolution

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, native enzyme

Released:
Source organism: Synechocystis sp. PCC 6803
Primary publication:
The structure of a retinal-forming carotenoid oxygenase.
Science 308 267-9 (2005)
PMID: 15821095

Function and Biology Details

Reaction catalysed:
All-trans-8'-apo-beta-carotenal + O(2) = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-159934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apocarotenoid-15,15'-oxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 490 amino acids
Theoretical weight: 54.34 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P74334 (Residues: 1-490; Coverage: 100%)
Gene name: sll1541
Sequence domains: Retinal pigment epithelial membrane protein

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 119.046Å b: 125.278Å c: 203.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.224
Expression system: Escherichia coli BL21(DE3)