› 1m1o

X-ray diffraction
1.95Å resolution

Crystal structure of biosynthetic thiolase, C89A mutant, complexed with acetoacetyl-CoA

Released:
DOI: 10.2210/pdb1m1o/pdb
PDB entry 1m1o coloured by chain, front view.
PDB entry 1m1o coloured by chain, side view.
PDB entry 1m1o coloured by chain, top view.
Source organism: Zoogloea ramigera
Primary publication:
The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes.
Kursula P, Ojala J, Lambeir AM, Wierenga RK
Biochemistry 41 15543-56 (2002)
PMID: 12501183

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: 392 amino acids
Theoretical weight: 40.51 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 CAA 2 x CAA
1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 84.219Å b: 79.219Å c: 148.288Å
α: 90° β: 92.48° γ: 90°
R-values:
R R work R free
0.213 0.211 0.258
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Ubiquitin: structures, functions, mechanisms.
Pickart et al. (2004)
3 more

2 mentions without citation

The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities.
Kiema et al. (2014)
1 more