› 2wku

X-ray diffraction
2.3Å resolution

BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT.

Released:
DOI: 10.2210/pdb2wku/pdb
PDB entry 2wku coloured by chain, front view.
PDB entry 2wku coloured by chain, side view.
PDB entry 2wku coloured by chain, top view.
Source organism: Zoogloea ramigera
Primary publication:
The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation.
Meriläinen G, Poikela V, Kursula P, Wierenga RK
Biochemistry 48 11011-25 (2009)
PMID: 19842716

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: 40.57 KDa
Source organism: Zoogloea ramigera
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07097 (Residues: 2-11, 12-392; Coverage: 100%)
Gene names: phaA, phbA
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand SO4 9 x SO4
Ligand DNO 4 x DNO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 84.5Å b: 79.5Å c: 147.7Å
α: 90° β: 91.5° γ: 90°
R-values:
R R work R free
0.204 0.201 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Specificity in transition state binding: the Pauling model revisited.
Amyes et al. (2013)
1 more