› 2rgh

X-ray diffraction
2.3Å resolution

Structure of Alpha-Glycerophosphate Oxidase from Streptococcus sp.: A Template for the Mitochondrial Alpha-Glycerophosphate Dehydrogenase

Released:
DOI: 10.2210/pdb2rgh/pdb
PDB entry 2rgh coloured by chain, front view.
PDB entry 2rgh coloured by chain, side view.
PDB entry 2rgh coloured by chain, top view.
Source organism: Streptococcus sp.
Primary publication:
Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase.
Colussi T, Parsonage D, Boles W, Matsuoka T, Mallett TC, Karplus PA, Claiborne A
Biochemistry 47 965-77 (2008)
PMID: 18154320

Function and Biology Details

Reaction catalysed: 
sn-glycerol 3-phosphate + O(2) = glycerone phosphate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112157 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-glycerophosphate oxidase Chain: A
Molecule details ›
Chain: A
Length: 571 amino acids
Theoretical weight: 64.25 KDa
Source organism: Streptococcus sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VWY7 (Residues: 1-557; Coverage: 100%)
Gene name: glpO
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 13 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21212
Unit cell:
a: 86.28Å b: 95.55Å c: 77.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.21 0.253
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues.
Mráček et al. (2013)
2 more

6 mentions without citation

Metformin suppresses gluconeogenesis by inhibiting mitochondrial glycerophosphate dehydrogenase.
Madiraju et al. (2014)
5 more