1.8.5.7: glutathionyl-hydroquinone reductase
This is an abbreviated version!
For detailed information about glutathionyl-hydroquinone reductase, go to the full flat file.
Reaction
Synonyms
ECM4, GHR1, glutathionyl-hydroquinone lyase, glutathionyl-hydroquinone reductase, nmagghr, Nmag_1170, NmGHR, pcpF, Xi class glutathione transferase, Xi class GST, yqjG
ECTree
1.8.5.7 glutathionyl-hydroquinone reductaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 1.8.5.7 - glutathionyl-hydroquinone reductase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
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
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
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
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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
