› 1g3l

X-ray diffraction
2.7Å resolution

THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-L-RHAMNOSE COMPLEX.

Released:
DOI: 10.2210/pdb1g3l/pdb
PDB entry 1g3l coloured by chain, front view.
PDB entry 1g3l coloured by chain, side view.
PDB entry 1g3l coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
Blankenfeldt W, Asuncion M, Lam JS, Naismith JH
EMBO J 19 6652-63 (2000)
PMID: 11118200

Function and Biology Details

Reaction catalysed: 
dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphate thymidylyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 293 amino acids
Theoretical weight: 32.49 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HU22 (Residues: 1-293; Coverage: 100%)
Gene names: PA5163, rmlA
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand TRH 8 x TRH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 71.087Å b: 138.557Å c: 139.676Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.23
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Review: Lipopolysaccharide biosynthesis in Pseudomonas aeruginosa.
King et al. (2009)
9 more

9 mentions without citation

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