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Updated: Oct 13, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida

H Motoshima1, K Inagaki, T Kumasaka

  • 1RIKEN Harima Institute, Kouto, Mikazuki, Sayo-gun, Hyogo 679-5148, Japan.

Journal of Biochemistry
|August 31, 2000
PubMed

Insights

This study determined the crystal structures of L-methionine gamma-lyase (MGL) from Pseudomonas putida. The findings reveal its homotetrameric structure and domain arrangement, offering insights into enzyme function.

Area of Science:

  • Enzymology
  • Structural Biology
  • Biochemistry

Background:

  • L-methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme.
  • MGL catalyzes the alpha,gamma-elimination of L-methionine, a key reaction in amino acid metabolism.

Purpose of the Study:

  • To elucidate the three-dimensional structure of MGL from Pseudomonas putida.
  • To understand the structural basis of MGL's catalytic mechanism and substrate specificity.

Main Methods:

  • Determined two crystal structures of MGL using multiwavelength anomalous diffraction (MAD) and molecular replacement.
  • Refined structures to 2.0 and 1.7 Å resolution using synchrotron radiation diffraction data.

Main Results:

  • Revealed a homotetrameric quaternary structure with 222 symmetry.
  • Identified active dimers formed by two associated monomers.
  • Observed a spatial fold with three distinct domains, similar to related enzymes like L-cystathionine beta-lyase.

Conclusions:

  • The determined structures provide a detailed molecular model of MGL.
  • Structural similarities suggest conserved mechanisms among PLP-dependent lyases.
  • Insights into MGL structure can guide future studies on enzyme engineering and drug design.

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