› 1yp4

X-ray diffraction
2.3Å resolution

Crystal structure of potato tuber ADP-glucose pyrophosphorylase in complex with ADP-glucose

Released:
DOI: 10.2210/pdb1yp4/pdb
PDB entry 1yp4 coloured by chain, front view.
PDB entry 1yp4 coloured by chain, side view.
PDB entry 1yp4 coloured by chain, top view.
Source organism: Solanum tuberosum
Primary publication:
Crystal structure of potato tuber ADP-glucose pyrophosphorylase.
Jin X, Ballicora MA, Preiss J, Geiger JH
EMBO J 24 694-704 (2005)
PMID: 15692569

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149989 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 451 amino acids
Theoretical weight: 49.8 KDa
Source organism: Solanum tuberosum
Expression system: Escherichia coli
UniProt:
  • Canonical: P23509 (Residues: 72-521; Coverage: 86%)
Sequence domains: Nucleotidyl transferase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 16 x SO4
Ligand ADP 2 x ADP
Ligand ADQ 1 x ADQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21
Unit cell:
a: 79.857Å b: 137.964Å c: 90.832Å
α: 90° β: 112.91° γ: 90°
R-values:
R R work R free
0.197 0.183 0.244
Expression system: Escherichia coli

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Citations

6 review citations

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

6 mentions without citation

Ostreococcus tauri ADP-glucose pyrophosphorylase reveals alternative paths for the evolution of subunit roles.
Kuhn et al. (2009)
5 more