› 3v8y

X-ray diffraction
2.15Å resolution

Structure of apo-glycogenin truncated at residue 270

Released:
DOI: 10.2210/pdb3v8y/pdb
PDB entry 3v8y coloured by chain, front view.
PDB entry 3v8y coloured by chain, side view.
PDB entry 3v8y coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.
Carrizo ME, Romero JM, Issoglio FM, Curtino JA
FEBS Lett 586 254-7 (2012)
PMID: 22226635

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-146532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycogenin-1 Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 32.61 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13280 (Residues: 1-271; Coverage: 81%)
Gene names: GYG, GYG1
Sequence domains: Glycosyl transferase family 8
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: I222
Unit cell:
a: 57.63Å b: 104.22Å c: 120.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.206 0.239
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

LC-MS/MS characterization of combined glycogenin-1 and glycogenin-2 enzymatic activities reveals their self-glucosylation preferences.
Nilsson et al. (2014)