› 2ib8

X-ray diffraction
1.85Å 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/pdb2ib8/pdb
PDB entry 2ib8 coloured by chain, front view.
PDB entry 2ib8 coloured by chain, side view.
PDB entry 2ib8 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: 41.53 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

4 bound ligands:
Ligand CL 4 x CL
Ligand K 4 x K
Ligand MES 4 x MES
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 75.651Å b: 107.277Å c: 102.209Å
α: 90° β: 103.07° γ: 90°
R-values:
R R work R free
0.164 0.162 0.205
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

6 mentions without citation

Site-specific reactivity of nonenzymatic lysine acetylation.
Baeza et al. (2015)
5 more