› 2vu0

X-ray diffraction
1.87Å resolution

Biosynthetic thiolase from Z. ramigera. Complex of the oxidised enzyme with coenzyme A.

Released:
DOI: 10.2210/pdb2vu0/pdb
PDB entry 2vu0 coloured by chain, front view.
PDB entry 2vu0 coloured by chain, side view.
PDB entry 2vu0 coloured by chain, top view.
Source organism: Zoogloea ramigera
Primary publication:
The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme.
Meriläinen G, Schmitz W, Wierenga RK, Kursula P
FEBS J 275 6136-48 (2008)
PMID: 19016856

Function and Biology Details

Reaction catalysed: 
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA acetyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 392 amino acids
Theoretical weight: 40.56 KDa
Source organism: Zoogloea ramigera
Expression system: Escherichia coli
UniProt:
  • Canonical: P07097 (Residues: 2-10, 11-392; Coverage: 100%)
Gene names: phaA, phbA
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 2 x COA
2 bound ligands:
Ligand GOL 1 x GOL
Ligand SO4 4 x SO4
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 84.402Å b: 79.056Å c: 148.802Å
α: 90° β: 92.66° γ: 90°
R-values:
R R work R free
0.195 0.194 0.229
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches.
Fox et al. (2014)
1 more