› 3usr

X-ray diffraction
2.1Å resolution

Structure of Y194F glycogenin mutant truncated at residue 270

Released:
DOI: 10.2210/pdb3usr/pdb
PDB entry 3usr coloured by chain, front view.
PDB entry 3usr coloured by chain, side view.
PDB entry 3usr coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Mechanisms of monomeric and dimeric glycogenin autoglucosylation.
Issoglio FM, Carrizo ME, Romero JM, Curtino JA
J Biol Chem 287 1955-61 (2012)
PMID: 22128147

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: 32.59 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: 58.28Å b: 103.37Å c: 119.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.239
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Vertebrate protein glycosylation: diversity, synthesis and function.
Moremen et al. (2012)
3 more

1 mention without citation

Mechanisms of monomeric and dimeric glycogenin autoglucosylation.
Issoglio et al. (2012)