› 3hl4

X-ray diffraction
2.2Å resolution

Crystal structure of a mammalian CTP:phosphocholine cytidylyltransferase with CDP-choline

Released:
DOI: 10.2210/pdb3hl4/pdb
PDB entry 3hl4 coloured by chain, front view.
PDB entry 3hl4 coloured by chain, side view.
PDB entry 3hl4 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold.
Lee J, Johnson J, Ding Z, Paetzel M, Cornell RB
J Biol Chem 284 33535-48 (2009)
PMID: 19783652

Function and Biology Details

Reaction catalysed: 
CTP + phosphocholine = diphosphate + CDP-choline
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Choline-phosphate cytidylyltransferase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 26.79 KDa
Source organism: Rattus norvegicus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P19836 (Residues: 1-236; Coverage: 64%)
Gene names: Ctpct, Pcyt1, Pcyt1a
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

3 bound ligands:
Ligand CDC 2 x CDC
Ligand GOL 1 x GOL
Ligand FMT 7 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21212
Unit cell:
a: 88.973Å b: 129.348Å c: 43.565Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.22 0.266
Expression system: Trichoplusia ni

Quick links

Citations

4 review citations

Phosphatidylcholine and the CDP-choline cycle.
Fagone et al. (2013)
3 more

10 mentions without citation

Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold.
Lee et al. (2009)
9 more