› 1ik4

X-ray diffraction
2Å resolution

X-ray Structure of Methylglyoxal Synthase from E. coli Complexed with Phosphoglycolohydroxamic Acid

Released:
DOI: 10.2210/pdb1ik4/pdb
PDB entry 1ik4 coloured by chain, front view.
PDB entry 1ik4 coloured by chain, side view.
PDB entry 1ik4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy.
Marks GT, Harris TK, Massiah MA, Mildvan AS, Harrison DH
Biochemistry 40 6805-18 (2001)
PMID: 11389594

Function and Biology Details

Reaction catalysed: 
Glycerone phosphate = methylglyoxal + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141519 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylglyoxal synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 152 amino acids
Theoretical weight: 16.94 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A731 (Residues: 1-152; Coverage: 100%)
Gene names: JW5129, b0963, mgsA, yccG
Sequence domains: MGS-like domain
Structure domains: Methylglyoxal synthase-like domain

Ligands and Environments

1 bound ligand:
Ligand PGH 6 x PGH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 53.05Å b: 129.53Å c: 178.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.169 0.206
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

The possible role of methylglyoxal metabolism in cancer.
Alfarouk et al. (2021)
13 other articles

1 mention without citation

Structural basis for the regulatory interaction of the methylglyoxal synthase MgsA with the carbon flux regulator Crh in Bacillus subtilis.
Dickmanns et al. (2018)