› 5k3j

X-ray diffraction
2.68Å resolution

Crystals structure of Acyl-CoA oxidase-2 in Caenorhabditis elegans bound with FAD, ascaroside-CoA, and ATP

Released:
DOI: 10.2210/pdb5k3j/pdb
PDB entry 5k3j coloured by chain, front view.
PDB entry 5k3j coloured by chain, side view.
PDB entry 5k3j coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Structural characterization of acyl-CoA oxidases reveals a direct link between pheromone biosynthesis and metabolic state in Caenorhabditis elegans.
Zhang X, Li K, Jones RA, Bruner SD, Butcher RA
Proc Natl Acad Sci U S A 113 10055-60 (2016)
PMID: 27551084

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-coenzyme A oxidase acox-1.2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 674 amino acids
Theoretical weight: 76.73 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O62137 (Residues: 1-661; Coverage: 100%)
Gene names: F08A8.2, acox-1.2, acox-2
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FAD 2 x FAD
Ligand ATP 2 x ATP
Ligand 6QA 2 x 6QA
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 76.04Å b: 85.571Å c: 106.899Å
α: 90° β: 91.43° γ: 90°
R-values:
R R work R free
0.215 0.213 0.245
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Decoding chemical communication in nematodes.
Butcher RA. (2017)
2 more

1 mention without citation

Structural characterization of acyl-CoA oxidases reveals a direct link between pheromone biosynthesis and metabolic state in Caenorhabditis elegans.
Zhang et al. (2016)