4uss

Populus trichocarpa glutathione transferase X1-1 (GHR1), complexed with glutathione

spinqualitylabelsall models 4uss, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uss is a 1 chain structure with sequence from Populus trichocarpa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: GSH, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Glutathionyl-hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt-GHR1 and Pt-GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt-GHR2 localizes in nucleoids. At the structural level, Pt-GHR1 adopts a typical GHR fold, with a dimerization interface comparable to that of the bacterial and fungal GHR counterparts. Pt-GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms. Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.,Lallement PA, Meux E, Gualberto JM, Dumarcay S, Favier F, Didierjean C, Saul F, Haouz A, Morel-Rouhier M, Gelhaye E, Rouhier N, Hecker A FEBS Lett. 2014 Nov 29. pii: S0014-5793(14)00826-6. doi:, 10.1016/j.febslet.2014.11.021. PMID:25455804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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