› 1g1l

X-ray diffraction
1.77Å resolution

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

Released:
DOI: 10.2210/pdb1g1l/pdb
PDB entry 1g1l coloured by chain, front view.
PDB entry 1g1l coloured by chain, side view.
PDB entry 1g1l 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: 32.49 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

3 bound ligands:
Ligand SO4 23 x SO4
Ligand DAU 16 x DAU
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 71.575Å b: 73.41Å c: 134.29Å
α: 89.94° β: 80.61° γ: 80.93°
R-values:
R R work R free
0.159 0.156 0.215
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

6 mentions without citation

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