› 2jl4

X-ray diffraction
2.3Å resolution

Holo structure of Maleyl Pyruvate Isomerase, a bacterial glutathione- s-transferase in Zeta class

Released:
DOI: 10.2210/pdb2jl4/pdb
PDB entry 2jl4 coloured by chain, front view.
PDB entry 2jl4 coloured by chain, side view.
PDB entry 2jl4 coloured by chain, top view.
Source organism: Ralstonia sp. U2
Primary publication:
Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase and implications for mechanism of isomerisation.
Marsh M, Shoemark DK, Jacob A, Robinson C, Cahill B, Zhou NY, Williams PA, Hadfield AT
J Mol Biol 384 165-77 (2008)
PMID: 18824004

Function and Biology Details

Reaction catalysed: 
3-maleylpyruvate = 3-fumarylpyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131451 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maleylpyruvate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 23.66 KDa
Source organism: Ralstonia sp. U2
Expression system: Escherichia coli
UniProt:
  • Canonical: O86043 (Residues: 1-212; Coverage: 100%)
Gene name: nagL
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P212121
Unit cell:
a: 60.332Å b: 81.733Å c: 88.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.267
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
4 more