› 1m3z

X-ray diffraction
1.87Å resolution

Biosynthetic thiolase, C89A mutant, complexed with acetyl coenzyme A

Released:
DOI: 10.2210/pdb1m3z/pdb
PDB entry 1m3z coloured by chain, front view.
PDB entry 1m3z coloured by chain, side view.
PDB entry 1m3z 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 ACO 4 x ACO
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: 84.6Å b: 79.68Å c: 149.321Å
α: 90° β: 92.83° γ: 90°
R-values:
R R work R free
0.195 0.192 0.242
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

2 mentions without citation

Quantitative Characterization of Configurational Space Sampled by HIV-1 Nucleocapsid Using Solution NMR, X-ray Scattering and Protein Engineering.
Deshmukh et al. (2016)
1 more