› 2gwc

X-ray diffraction
2.18Å resolution

Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue

Released:
DOI: 10.2210/pdb2gwc/pdb
PDB entry 2gwc coloured by chain, front view.
PDB entry 2gwc coloured by chain, side view.
PDB entry 2gwc coloured by chain, top view.
Source organism: Brassica juncea
Primary publication:
Structural basis for the redox control of plant glutamate cysteine ligase.
Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K
J Biol Chem 281 27557-65 (2006)
PMID: 16766527

Function and Biology Details

Reaction catalysed: 
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--cysteine ligase, chloroplastic Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 449 amino acids
Theoretical weight: 51.82 KDa
Source organism: Brassica juncea
Expression system: Escherichia coli
UniProt:
  • Canonical: O23736 (Residues: 66-514; Coverage: 87%)
Gene names: ECS1, GSH1
Sequence domains: Glutamate-cysteine ligase family 2(GCS2)
Structure domains: Creatine Kinase; Chain A, domain 2

Ligands and Environments

2 bound ligands:
Ligand MG 8 x MG
Ligand BSC 8 x BSC
1 modified residue:
Ligand MSE 144 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 88.04Å b: 198.92Å c: 114.97Å
α: 90° β: 99.66° γ: 90°
R-values:
R R work R free
0.2 0.198 0.241
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Redox regulation in photosynthetic organisms: signaling, acclimation, and practical implications.
Foyer et al. (2009)
21 more