› 1evj

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D

Released:
DOI: 10.2210/pdb1evj/pdb
PDB entry 1evj coloured by chain, front view.
PDB entry 1evj coloured by chain, side view.
PDB entry 1evj coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN
J Mol Biol 304 575-84 (2000)
PMID: 11099381

Function and Biology Details

Reaction catalysed: 
D-glucose + D-fructose = D-gluconolactone + D-glucitol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170577 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose--fructose oxidoreductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 352 amino acids
Theoretical weight: 39.26 KDa
Source organism: Zymomonas mobilis
Expression system: Zymomonas mobilis
UniProt:
  • Canonical: Q07982 (Residues: 82-433; Coverage: 92%)
Gene names: ZMO0689, gfo
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 47.71Å b: 91.46Å c: 98.92Å
α: 64.53° β: 84.45° γ: 75.28°
R-values:
R R work R free
0.241 0.241 0.284
Expression system: Zymomonas mobilis

Quick links

Citations

5 citation in other articles

Gal80 dimerization and the yeast GAL gene switch.
Pilauri et al. (2005)
4 more

1 mention without citation

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases.
Taberman et al. (2016)