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Structure of methionine γ-lyase from Clostridium sporogenes

Svetlana Revtovich1, Natalya Anufrieva1, Elena Morozova1

  • 1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.

Acta Crystallographica. Section F, Structural Biology Communications
|January 12, 2016
PubMed

Insights

The crystal structure of Methionine γ-lyase (MGL) from Clostridium sporogenes was determined. This pyridoxal 5′-phosphate-dependent enzyme is a potential therapeutic target for anaerobic pathogens and cancer.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Methionine γ-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme.
  • MGL catalyzes the γ-elimination reaction of L-methionine.
  • MGL is a potential therapeutic target for anaerobic pathogens and cancer.

Purpose of the Study:

  • Determine the crystal structure of MGL from Clostridium sporogenes.
  • Compare the structure of MGL with homologous enzymes.
  • Identify structural differences relevant to active-site architecture.

Main Methods:

  • X-ray crystallography
  • Protein structure determination
  • Structural comparison

Main Results:

  • The crystal structure of MGL from Clostridium sporogenes was determined at 2.37 Å resolution.
  • The overall fold of MGL is similar to homologous enzymes from other species.
  • Differences in flexible regions of N- and C-terminal domains affect active-site architecture.

Conclusions:

  • The determined MGL structure provides insights into its active-site architecture.
  • Structural variations may influence enzyme activity and substrate specificity.
  • Further studies can leverage this structural information for therapeutic development.
Keywords:
Clostridium sporogenesactive sitemethionine γ-lyasepyridoxal 5′-phosphate-binding sitetetrameric contacts

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