› 1rzu

X-ray diffraction
2.3Å resolution

Crystal structure of the glycogen synthase from A. tumefaciens in complex with ADP

Released:
DOI: 10.2210/pdb1rzu/pdb
PDB entry 1rzu coloured by chain, front view.
PDB entry 1rzu coloured by chain, side view.
PDB entry 1rzu coloured by chain, top view.
Source organism: Agrobacterium tumefaciens
Primary publication:
Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation.
Buschiazzo A, Ugalde JE, Guerin ME, Shepard W, Ugalde RA, Alzari PM
EMBO J 23 3196-205 (2004)
PMID: 15272305

Function and Biology Details

Reaction catalysed: 
ADP-alpha-D-glucose + ((1->4)-alpha-D-glucosyl)(n) = ADP + ((1->4)-alpha-D-glucosyl)(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogen synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 485 amino acids
Theoretical weight: 52.46 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A3F3 (Residues: 1-480; Coverage: 100%)
Gene names: glgA, glgA1
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 69.357Å b: 88.115Å c: 84.463Å
α: 90° β: 98.19° γ: 90°
R-values:
R R work R free
0.184 0.18 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
14 more

9 mentions without citation

Potato starch synthases: Functions and relationships.
Nazarian-Firouzabadi et al. (2017)
8 more