› 4uss

X-ray diffraction
2.5Å resolution

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

Released:
DOI: 10.2210/pdb4uss/pdb
PDB entry 4uss coloured by chain, front view.
PDB entry 4uss coloured by chain, side view.
PDB entry 4uss coloured by chain, top view.
Source organism: Populus trichocarpa
Primary publication:
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 589 37-44 (2015)
PMID: 25455804

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GLUTATHIONYL HYDROQUINONE REDUCTASE Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.18 KDa
Source organism: Populus trichocarpa
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GSH 1 x GSH
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 36.53Å b: 92.409Å c: 86.901Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.233
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Plant glutathione transferase-mediated stress tolerance: functions and biotechnological applications.
Nianiou-Obeidat et al. (2017)
1 more

2 mentions without citation

Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.
Schwartz et al. (2016)
1 more