› 1v4g

X-ray diffraction
2.5Å resolution

Crystal Structure of gamma-Glutamylcysteine Synthetase from Escherichia coli B

Released:
DOI: 10.2210/pdb1v4g/pdb
PDB entry 1v4g coloured by chain, front view.
PDB entry 1v4g coloured by chain, side view.
PDB entry 1v4g coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.
Hibi T, Nii H, Nakatsu T, Kimura A, Kato H, Hiratake J, Oda J
Proc Natl Acad Sci U S A 101 15052-7 (2004)
PMID: 15477603

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--cysteine ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 518 amino acids
Theoretical weight: 58.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6W9 (Residues: 1-518; Coverage: 100%)
Gene names: JW2663, b2688, gsh-I, gshA
Sequence domains: Glutamate-cysteine ligase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand FME 4 x FME

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: R3
Unit cell:
a: 326.818Å b: 326.818Å c: 104.726Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.206 0.236
Expression system: Escherichia coli

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Citations

12 review citations

Redox-directed cancer therapeutics: molecular mechanisms and opportunities.
Wondrak GT. (2009)
11 more

2 mentions without citation

Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights.
Krajewski et al. (2005)
1 more