› 1xmd

X-ray diffraction
2.1Å resolution

M335V mutant structure of mouse carnitine octanoyltransferase

Released:
DOI: 10.2210/pdb1xmd/pdb
PDB entry 1xmd coloured by chain, front view.
PDB entry 1xmd coloured by chain, side view.
PDB entry 1xmd coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity.
Jogl G, Hsiao YS, Tong L
J Biol Chem 280 738-44 (2005)
PMID: 15492013

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190101 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal carnitine O-octanoyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 612 amino acids
Theoretical weight: 70.33 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9DC50 (Residues: 1-612; Coverage: 100%)
Gene names: Cot, Crot
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand EPE 2 x EPE
Ligand MPD 7 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: R3
Unit cell:
a: 164Å b: 164Å c: 159.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.224
Expression system: Escherichia coli

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Citations

2 review citations

Acyl-CoA metabolism and partitioning.
Grevengoed et al. (2014)
1 more