› 1g23

X-ray diffraction
2.8Å resolution

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

Released:
DOI: 10.2210/pdb1g23/pdb
PDB entry 1g23 coloured by chain, front view.
PDB entry 1g23 coloured by chain, side view.
PDB entry 1g23 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, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 293 amino acids
Theoretical weight: 32.68 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 G1P 8 x G1P
Ligand SO4 13 x SO4
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P1
Unit cell:
a: 71.583Å b: 73.901Å c: 133.748Å
α: 89.81° β: 80.31° γ: 80.18°
R-values:
R R work R free
0.201 0.199 0.226
Expression system: Escherichia coli

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Citations

11 review citations

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

7 mentions without citation

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