› 3s20

X-ray diffraction
1.88Å resolution

Crystal structure of cerulenin bound Xanthomonas campestri OleA (soak)

Released:
DOI: 10.2210/pdb3s20/pdb
PDB entry 3s20 coloured by chain, front view.
PDB entry 3s20 coloured by chain, side view.
PDB entry 3s20 coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris
Primary publication:
Crystal structures of Xanthomonas campestris OleA reveal features that promote head-to-head condensation of two long-chain fatty acids.
Goblirsch BR, Frias JA, Wackett LP, Wilmot CM
Biochemistry 51 4138-46 (2012)
PMID: 22524624

Function and Biology Details

Reaction catalysed: 
2 an acyl-CoA + H(2)O = a (2R)-2-alkyl-3-oxoalkanoate + 2 CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-CoA:acyl-CoA alkyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 37.31 KDa
Source organism: Xanthomonas campestris pv. campestris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8PDX2 (Residues: 1-338; Coverage: 100%)
Gene names: XCC0212, oleA
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand CER 2 x CER
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 81.653Å b: 85.358Å c: 103.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.2
Expression system: Escherichia coli

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Citations

4 review citations

Enzymes for fatty acid-based hydrocarbon biosynthesis.
Herman et al. (2016)
3 more