› 2gwd

X-ray diffraction
2.09Å resolution

Crystal structure of plant glutamate cysteine ligase in complex with Mg2+ and L-glutamate

Released:
DOI: 10.2210/pdb2gwd/pdb
PDB entry 2gwd coloured by chain, front view.
PDB entry 2gwd coloured by chain, side view.
PDB entry 2gwd 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 Chain: A
Molecule details ›
Chain: A
Length: 449 amino acids
Theoretical weight: 50.97 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

3 bound ligands:
Ligand MG 1 x MG
Ligand ACT 5 x ACT
Ligand GLU 1 x GLU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6122
Unit cell:
a: 54.81Å b: 54.81Å c: 518.04Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.175 0.227
Expression system: Escherichia coli

Quick links

Citations

23 review citations

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

5 mentions without citation

The pupylation pathway and its role in mycobacteria.
Barandun et al. (2012)
4 more