› 1n1d

X-ray diffraction
2Å resolution

Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol

Released:
DOI: 10.2210/pdb1n1d/pdb
PDB entry 1n1d coloured by chain, front view.
PDB entry 1n1d coloured by chain, side view.
PDB entry 1n1d coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis.
Pattridge KA, Weber CH, Friesen JA, Sanker S, Kent C, Ludwig ML
J Biol Chem 278 51863-71 (2003)
PMID: 14506262

Function and Biology Details

Reaction catalysed: 
CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151043 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol-3-phosphate cytidylyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 129 amino acids
Theoretical weight: 15.3 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P27623 (Residues: 1-129; Coverage: 100%)
Gene names: BSU35740, tagD
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand C2G 4 x C2G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 37.795Å b: 55.929Å c: 63.701Å
α: 88.99° β: 75.03° γ: 82.54°
R-values:
R R work R free
0.246 0.241 0.294
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The Kennedy pathway--De novo synthesis of phosphatidylethanolamine and phosphatidylcholine.
Gibellini et al. (2010)
1 more

6 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)
5 more