› 1mc3

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF RFFH

Released:
DOI: 10.2210/pdb1mc3/pdb
PDB entry 1mc3 coloured by chain, front view.
PDB entry 1mc3 coloured by chain, side view.
PDB entry 1mc3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+.
Sivaraman J, Sauvé V, Matte A, Cygler M
J Biol Chem 277 44214-9 (2002)
PMID: 12171937

Function and Biology Details

Reaction catalysed: 
dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphate thymidylyltransferase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 33.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P61887 (Residues: 1-293; Coverage: 100%)
Gene names: JW3763, b3789, rffH, rmlA2, yifG
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand TTP 2 x TTP
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 144.338Å b: 71.682Å c: 59.413Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.28
Expression system: Escherichia coli

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Citations

4 review citations

ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis.
Ballicora et al. (2003)
3 more

8 mentions without citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
7 more