EC Number   |
|---|
  1.8.5.7 | binary complex structure with glutathionyl-menadione. The structure reveals a large H-site that could accommodate various substituted hydroquinones and a hydrogen network of three Tyr residues that could provide the proton for reductive deglutathionylation |
| 1.8.5.7 | isoform ECM4 shows extensions including a huge loop which contributes to the quaternary assembly. Soaking of ECM4 crystals with glutathionyl-menadione results in a structure where glutathione forms a mixed disulfide bond with the cysteine 46. Residues H345 and H350, F228, Y224 and W48 could play crucial roles in binding of glutathionyl-(hydro)quinones, and in assisting C46 during catalysis |
| 1.8.5.7 | purified enzyme in apoform, mixing of 0.5 ml of 6.6 mg/ml protein in 50 mM Tris-HCl, pH 7.5, and 3.5 M NaCl, with 0.5 ml of reservoir solution containing 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, and 0.2 M lithium sulfate, at 21°C, X-ray diffraction structure determination and analysis at 2.61 A resolution, molecular replacement using the structure of monomeric putative GST from Corynebacterium glutamicum (PDB ID 3M1G) as a search model, model building |
| 1.8.5.7 | structure in complex with glutathione, to 2.5 A resolution. Isoform GHR1 adopts a typical glutathionyl-hydroquinone reductase fold, with a dimerization interface comparable to that of the bacterial and fungal counterparts |
