› 1qfl

X-ray diffraction
1.92Å resolution

BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH A REACTION INTERMEDIATE.

Released:
DOI: 10.2210/pdb1qfl/pdb
PDB entry 1qfl coloured by chain, front view.
PDB entry 1qfl coloured by chain, side view.
PDB entry 1qfl coloured by chain, top view.
Source organism: Zoogloea ramigera
Primary publication:
A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism.
Modis Y, Wierenga RK
Structure 7 1279-90 (1999)
PMID: 10545327

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 domain:

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: 389 amino acids
Theoretical weight: 40.3 KDa
Source organism: Zoogloea ramigera
Expression system: Escherichia coli
UniProt:
  • Canonical: P07097 (Residues: 5-11, 12-392; Coverage: 99%)
Gene names: phaA, phbA
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 4 x COA
1 bound ligand:
Ligand SO4 6 x SO4
1 modified residue:
Ligand SCY 4 x SCY

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P21
Unit cell:
a: 84.459Å b: 78.864Å c: 149.745Å
α: 90° β: 93.43° γ: 90°
R-values:
R R work R free
0.209 0.209 0.256
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The thiolase superfamily: condensing enzymes with diverse reaction specificities.
Haapalainen et al. (2006)
3 more

2 mentions without citation

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.
Ishikawa et al. (2004)
1 more