› 1t7n

X-ray diffraction
1.9Å resolution

Crystal structure of the M564G mutant of murine CrAT

Released:
DOI: 10.2210/pdb1t7n/pdb
PDB entry 1t7n coloured by chain, front view.
PDB entry 1t7n coloured by chain, side view.
PDB entry 1t7n 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 Chain: A
Molecule details ›
Chain: A
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P43
Unit cell:
a: 72.19Å b: 72.19Å c: 128.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.185 0.218
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