› 2icy

X-ray diffraction
1.64Å resolution

Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UDP-glucose

Released:
DOI: 10.2210/pdb2icy/pdb
PDB entry 2icy coloured by chain, ensemble of 2 models, front view.
PDB entry 2icy coloured by chain, ensemble of 2 models, side view.
PDB entry 2icy coloured by chain, ensemble of 2 models, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.
McCoy JG, Bitto E, Bingman CA, Wesenberg GE, Bannen RM, Kondrashov DA, Phillips GN
J Mol Biol 366 830-41 (2007)
PMID: 17178129

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192383 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UTP--glucose-1-phosphate uridylyltransferase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 469 amino acids
Theoretical weight: 51.75 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9M9P3 (Residues: 2-469; Coverage: 100%)
Gene names: At3g03250, T17B22.6, UGP2
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand DMS 1 x DMS
Ligand UPG 2 x UPG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 188.008Å b: 59.712Å c: 89.762Å
α: 90° β: 100.32° γ: 90°
R-values:
R R work R free
0.183 0.183 0.223
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Biochemistry and genetics of starch synthesis.
Keeling et al. (2010)
6 more

5 mentions without citation

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.
McCoy et al. (2007)
4 more