› 3ig8

X-ray diffraction
2.69Å resolution

Saccharomyces cerevisiae glutamate cysteine ligase in complex with Mg2+, L-glutamate and ADP

Released:
DOI: 10.2210/pdb3ig8/pdb
PDB entry 3ig8 coloured by chain, front view.
PDB entry 3ig8 coloured by chain, side view.
PDB entry 3ig8 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase.
Biterova EI, Barycki JJ
J Biol Chem 284 32700-8 (2009)
PMID: 19726687

Function and Biology Details

Reaction catalysed: 
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--cysteine ligase Chain: A
Molecule details ›
Chain: A
Length: 692 amino acids
Theoretical weight: 79.93 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32477 (Residues: 1-678; Coverage: 100%)
Gene names: GSH1, J0832, YJL101C
Sequence domains: Glutamate-cysteine ligase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand GLU 1 x GLU
Ligand ADP 1 x ADP
Ligand MG 3 x MG
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P43212
Unit cell:
a: 117.849Å b: 117.849Å c: 164.444Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.242
Expression system: Escherichia coli

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Citations

3 review citations

Emerging regulatory paradigms in glutathione metabolism.
Liu et al. (2014)
2 more

3 mentions without citation

Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase.
Biterova et al. (2009)
2 more