› 1m0w

X-ray diffraction
1.8Å resolution

Yeast Glutathione Synthase Bound to gamma-glutamyl-cysteine, AMP-PNP and 2 Magnesium Ions

Released:
DOI: 10.2210/pdb1m0w/pdb
PDB entry 1m0w coloured by chain, front view.
PDB entry 1m0w coloured by chain, side view.
PDB entry 1m0w coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Large conformational changes in the catalytic cycle of glutathione synthase.
Gogos A, Shapiro L
Structure 10 1669-76 (2002)
PMID: 12467574

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione synthetase GSH2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 491 amino acids
Theoretical weight: 55.88 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q08220 (Residues: 1-491; Coverage: 100%)
Gene names: GSH2, YOL049W
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand 3GC 2 x 3GC
3 bound ligands:
Ligand MG 4 x MG
Ligand SO4 7 x SO4
Ligand ANP 2 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 51.661Å b: 52.006Å c: 100.636Å
α: 82.08° β: 86.77° γ: 77.49°
R-values:
R R work R free
0.172 0.172 0.196
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

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

8 mentions without citation

Structural basis of tubulin tyrosination by tubulin tyrosine ligase.
Prota et al. (2013)
7 more