X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase from Listeria monocytogenes

Entry authors: Patskovsky Y, Ho J, Toro R, Gilmore M, Miller S, Groshong C, Sauder JM, Burley SK, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Ribitol-5-phosphate cytidylyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 27.93 KDa
Source organism: Listeria monocytogenes serotype 4b str. F2365
Expression system: Escherichia coli
  • Canonical: Q720Y7 (Residues: 2-236; Coverage: 99%)
Gene names: LMOf2365_1100, tarI
Sequence domains: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 157.202Å b: 45.938Å c: 79.007Å
α: 90° β: 108.89° γ: 90°
R R work R free
0.242 0.241 0.277
Expression system: Escherichia coli