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

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:,
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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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. Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones. FEBS Lett. 2014 Nov 29. pii: S0014-5793(14)00826-6. doi:, 10.1016/j.febslet.2014.11.021. PMID:25455804 doi:http://dx.doi.org/10.1016/j.febslet.2014.11.021

4uss, resolution 2.50Å

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