› 1h5t

X-ray diffraction
1.9Å resolution

Thymidylyltransferase complexed with Thymidylyldiphosphate-glucose

Released:
DOI: 10.2210/pdb1h5t/pdb
PDB entry 1h5t coloured by chain, front view.
PDB entry 1h5t coloured by chain, side view.
PDB entry 1h5t coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase.
Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M
J Mol Biol 313 831-43 (2001)
PMID: 11697907

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153476 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glucose-1-phosphate thymidylyltransferase 1 Chains: A, C, D
Molecule details ›
Chains: A, C, D
Length: 293 amino acids
Theoretical weight: 32.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37744 (Residues: 1-293; Coverage: 100%)
Gene names: JW2024, b2039, rfbA, rmlA, rmlA1
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Glucose-1-phosphate thymidylyltransferase 1 Chain: B
Molecule details ›
Chain: B
Length: 293 amino acids
Theoretical weight: 32.71 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P37744 (Residues: 1-293; Coverage: 100%)
Gene names: JW2024, b2039, rfbA, rmlA, rmlA1
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
Ligand TYD 4 x TYD
Ligand DAU 4 x DAU
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 72.81Å b: 119.49Å c: 81.17Å
α: 90° β: 112.67° γ: 90°
R-values:
R R work R free
0.174 0.174 0.224
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Biosynthesis of O-antigens: genes and pathways involved in nucleotide sugar precursor synthesis and O-antigen assembly.
Samuel et al. (2003)
6 more

9 mentions without citation

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