› 1t7q

X-ray diffraction
1.8Å resolution

Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA

Released:
DOI: 10.2210/pdb1t7q/pdb
PDB entry 1t7q coloured by chain, front view.
PDB entry 1t7q coloured by chain, side view.
PDB entry 1t7q coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase.
Hsiao YS, Jogl G, Tong L
J Biol Chem 279 31584-9 (2004)
PMID: 15155726

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: 618 amino acids
Theoretical weight: 70.02 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P47934 (Residues: 30-626; Coverage: 95%)
Gene name: Crat
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA
2 bound ligands:
Ligand 152 2 x 152
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 165.13Å b: 89.63Å c: 123.05Å
α: 90° β: 129.23° γ: 90°
R-values:
R R work R free
0.2 0.191 0.221
Expression system: Escherichia coli

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Citations

2 review citations

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