› 5lkd

X-ray diffraction
1.68Å resolution

Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae in complex with glutathione

Released:
DOI: 10.2210/pdb5lkd/pdb
PDB entry 5lkd coloured by chain, front view.
PDB entry 5lkd coloured by chain, side view.
PDB entry 5lkd coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.
Schwartz M, Didierjean C, Hecker A, Girardet JM, Morel-Rouhier M, Gelhaye E, Favier F
PLoS One 11 e0164678 (2016)
PMID: 27736955

Function and Biology Details

Reactions catalysed: 
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153138 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase omega-like 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 378 amino acids
Theoretical weight: 44.41 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P36156 (Residues: 1-370; Coverage: 100%)
Gene names: ECM4, GTO2, YKR076W
Sequence domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 55.44Å b: 82.44Å c: 80.58Å
α: 90° β: 95.31° γ: 90°
R-values:
R R work R free
0.161 0.159 0.2
Expression system: Escherichia coli

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Citations

2 review citations

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.
Sylvestre-Gonon et al. (2019)
1 more

1 mention without citation

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