› 2ibw

X-ray diffraction
1.9Å resolution

Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function

Released:
DOI: 10.2210/pdb2ibw/pdb
PDB entry 2ibw coloured by chain, front view.
PDB entry 2ibw coloured by chain, side view.
PDB entry 2ibw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function.
Haapalainen AM, Meriläinen G, Pirilä PL, Kondo N, Fukao T, Wierenga RK
Biochemistry 46 4305-21 (2007)
PMID: 17371050

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-150282 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA acetyltransferase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 395 amino acids
Theoretical weight: 41.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P24752 (Residues: 33-427; Coverage: 93%)
Gene names: ACAT, ACAT1, MAT
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 4 x COA
4 bound ligands:
Ligand CL 4 x CL
Ligand K 4 x K
Ligand MES 1 x MES
Ligand GOL 1 x GOL
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 76.143Å b: 107.577Å c: 101.954Å
α: 90° β: 102.89° γ: 90°
R-values:
R R work R free
0.155 0.153 0.194
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Role of de novo cholesterol synthesis enzymes in cancer.
Yang et al. (2020)
3 more

5 mentions without citation

Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.
Garrido Ruiz et al. (2022)
4 more