› 2c21

X-ray diffraction
2Å resolution

Specificity of the Trypanothione-dependednt Leishmania major Glyoxalase I: Structure and biochemical comparison with the human enzyme

Released:
DOI: 10.2210/pdb2c21/pdb
PDB entry 2c21 coloured by chain, front view.
PDB entry 2c21 coloured by chain, side view.
PDB entry 2c21 coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme.
Ariza A, Vickers TJ, Greig N, Armour KA, Dixon MJ, Eggleston IM, Fairlamb AH, Bond CS
Mol Microbiol 59 1239-48 (2006)
PMID: 16430697

Function and Biology Details

Reaction catalysed: 
(R)-S-lactoylglutathione = glutathione + methylglyoxal
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179350 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
lactoylglutathione lyase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 144 amino acids
Theoretical weight: 16.62 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q68RJ8 (Residues: 1-141; Coverage: 100%)
Gene names: GLO1, LMJF_35_3010
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

4 bound ligands:
Ligand NI 6 x NI
Ligand MPD 6 x MPD
Ligand MRD 2 x MRD
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 130.193Å b: 148.957Å c: 50.698Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.155 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

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

9 mentions without citation

Nonredox nickel enzymes.
Maroney et al. (2014)
8 more