› 3fro

X-ray diffraction
2.5Å resolution

Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations

Released:
DOI: 10.2210/pdb3fro/pdb
PDB entry 3fro coloured by chain, front view.
PDB entry 3fro coloured by chain, side view.
PDB entry 3fro coloured by chain, top view.
Source organism: Pyrococcus abyssi
Primary publication:
Lyase activity of glycogen synthase: Is an elimination/addition mechanism a possible reaction pathway for retaining glycosyltransferases?
Díaz A, Díaz-Lobo M, Grados E, Guinovart JJ, Fita I, Ferrer JC
IUBMB Life 64 649-58 (2012)
PMID: 22648728

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194179 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Starch synthase catalytic domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 439 amino acids
Theoretical weight: 49.34 KDa
Source organism: Pyrococcus abyssi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9V2J8 (Residues: 1-437; Coverage: 100%)
Gene name: PAB2292
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

3 bound ligands:
Ligand TRS 3 x TRS
Ligand PO4 3 x PO4
Ligand NHF 1 x NHF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 74.998Å b: 139.913Å c: 159.414Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.288 0.214 0.255
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Structural basis for 2'-phosphate incorporation into glycogen by glycogen synthase.
Chikwana et al. (2013)
4 more

1 mention without citation

Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM.
Syson et al. (2020)