4USS

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

Summary for 4USS

• Entry DOI: 10.2210/pdb4uss/pdb
• Descriptor: GLUTATHIONYL HYDROQUINONE REDUCTASE, GLUTATHIONE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: transferase, class xi, poplar, plastids
• Biological source: POPULUS TRICHOCARPA (BLACK COTTONWOOD)
• Total number of polymer chains: 1
• Total formula weight: 37678.02

Authors

Lallement, P.A.,Meux, E.,Gualberto, J.M.,Dumaracay, S.,Favier, F.,Didierjean, C.,Saul, F.,Haouz, A.,Morel-Rouhier, M.,Gelhaye, E.,Rouhier, N.,Hecker, A. (deposition date: 2014-07-13, release date: 2014-12-03, Last modification date: 2024-01-10)

Primary citation

Lallement, P.,Meux, E.,Gualberto, J.M.,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., 589:37-, 2015

PubMed Abstract: 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.

PubMed: 25455804
DOI: 10.1016/J.FEBSLET.2014.11.021

Experimental method

X-RAY DIFFRACTION (2.5 Å)