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1.8.1.7: glutathione-disulfide reductase

This is an abbreviated version!
For detailed information about glutathione-disulfide reductase, go to the full flat file.

Word Map on EC 1.8.1.7

Reaction

2 glutathione +

NADP+
=
glutathione disulfide
 +
NADPH
 +
H+

Synonyms

At3g54660, EC 1.6.4.2, GLR, glutahione reductase, glutathione disulfide reductase, glutathione reductase, glutathione reductase (NADPH), glutathione reductase 3, glutathione reductase Glr1, glutathione S-reductase, glutathione: NADP(+) oxidoreductase, glutathione: NADP+ oxidoreductase, glutathione:NADP+ oxidoreductase, Gor, GOR1, GOR2, GR, GR1, GR2, Gr3, GRase, GRase-1, GRd, GSH reductase, GSHR, Gsr, GSR-1, GSSG reductase, HCOI_01258400, hGR, HvGR1, HvGR2, multifunctional thioredoxin-glutathione reductase, NADPH-glutathione reductase, NADPH-GSSG reductase, NADPH-reduced GR, NADPH: oxidized glutathione oxidoreductase, NADPH:oxidized glutathione oxidoreductase, NADPH:oxidized-glutathione oxidoreductase, OBP29, PfGR, psgr, PtGR1.1, PtGR1.2, PtGR2, reductase, glutathione, SpGR, TaGR1, TaGR2, TGR, thioredoxin glutathione reductase, thioredoxin/glutathione reductase, TrxR3

ECTree

     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.7 glutathione-disulfide reductase

Crystallization

Crystallization on EC 1.8.1.7 - glutathione-disulfide reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling based on Trypanosoma brucei TPR protein, PDB ID 2WBA
hanging drop method, form-S grown crystals from salt and form-P grown crystals from PEG-8000, X-ray analysis
-
trigonal crystals, high internal symmetry
-
binding structure of diverse FAD analogues to the apoenzyme
-
dialysis for 72 h against 1000 volumes of deionized water with 1 change
-
hanging drop vapour diffusion method
-
molecular asymmetry of crystals from deionized water and from 2 M ammonium sulfate, exact 2fold molecular axis in the dimer, form A-D, three-dimensional structure
-
structure analysis overview, ligand binding, active center
-
substrate-binding and structure analysis
hanging drop vapour diffusion method
-
peroxynitrite inactivated enzyme, hanging drop vapour dffusion method, 10 mg/ml protein in 120 mM ammonium sulfate, 100 mM potassium phosphate, pH 7.5, against reservoir solution containing 720 mM ammonium sulfate, 100 mM potassium phosphate, pH 8.0, 30-37°C, 5 days, storage and handling in stabilization solution containing 1 M ammonium sulfate, 100 mM potassium phosphate, pH 8.0, X-ray structure determination and analysis at 1.9 A resolution
-
purified recombinant strain K1 wild-type enzyme, enzyme is dialyzed against EDTA for 3 h, hanging drop vapour diffusion method, protein solution contains 10 mg/ml protein, mixed with an equal volume of reservoir solution containing 14% w/v PEG monomethylether 550, 70 mM NaCl, 70 mM bicine, pH 8.7-9.0, 20°C, one week, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
-
hanging drop method, crystal structure is determined at 2.40 A resolution
hanging drop vapor diffusion method, using 22% (w/v) PEG 3350, 0.1 M HEPES pH 7.2, 0.2 M NaNO3, 5 mM dithiothreitol, or beta-mercaptoethanol
-
hanging-drop method at 22°C, size of crystals varies with ammonium sulfate concentration
-