› 2h3p

X-ray diffraction
2.2Å resolution

Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA

Released:
DOI: 10.2210/pdb2h3p/pdb
PDB entry 2h3p coloured by chain, front view.
PDB entry 2h3p coloured by chain, side view.
PDB entry 2h3p coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates.
Hsiao YS, Jogl G, Tong L
J Biol Chem 281 28480-7 (2006)
PMID: 16870616

Function and Biology Details

Reactions catalysed: 
Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
Acetyl-CoA + carnitine = CoA + O-acetylcarnitine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carnitine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 599 amino acids
Theoretical weight: 68.04 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P47934 (Residues: 30-625; Coverage: 95%)
Gene name: Crat
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO

Cofactor: Ligand COA 1 x COA
1 bound ligand:
Ligand 152 2 x 152
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 163.9Å b: 89.24Å c: 122.64Å
α: 90° β: 128.96° γ: 90°
R-values:
R R work R free
0.17 0.17 0.223
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural insight into function and regulation of carnitine palmitoyltransferase.
Rufer et al. (2009)
1 more

4 mentions without citation

Identification of a residue affecting fatty alcohol selectivity in wax ester synthase.
Barney et al. (2013)
3 more