› 5vxi

X-ray diffraction
2.08Å resolution

Crystal structure of Xanthomonas campestris OleA E117D bound with Cerulenin

Released:
DOI: 10.2210/pdb5vxi/pdb
PDB 5vxi coloured by chain and viewed from the front.
PDB 5vxi coloured by chain and viewed from the side.
PDB 5vxi coloured by chain and viewed from the top.
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Primary publication:
OleA Glu117 is key to condensation of two fatty-acyl coenzyme A substrates in long-chain olefin biosynthesis.
Jensen MR, Goblirsch BR, Christenson JK, Esler MA, Mohamed FA, Wackett LP, Wilmot CM
Biochem. J. (2017)
PMID: 29025976

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:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-CoA:acyl-CoA alkyltransferase Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 38.83 KDa
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Expression system: Escherichia coli BL21(DE3)
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 MN 1 x MN
Ligand CER 1 x CER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P3221
Unit cell:
a: 89.765Å b: 89.765Å c: 69.509Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.171 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

p-Nitrophenyl esters provide new insights and applications for the thiolase enzyme OleA.
Smith et al. (2021)
2 more