research communications
Methionine γ-lyase (MGL) is a pyridoxal 5′-phosphate-dependent enzyme that catalyzes the γ-elimination reaction of L-methionine. The enzyme is a promising target for therapeutic intervention in some anaerobic pathogens and has attracted interest as a potential cancer treatment. The crystal structure of MGL from Clostridium sporogenes has been determined at 2.37 Å resolution. The fold of the protein is similar to those of homologous enzymes from Citrobacter freundii, Entamoeba histolytica, Pseudomonas putida and Trichomonas vaginalis. A comparison of these structures revealed differences in the conformation of two flexible regions of the N- and C-terminal domains involved in the active-site architecture.
Keywords: methionine γ-lyase; active site; pyridoxal 5′-phosphate-binding site; tetrameric contacts; Clostridium sporogenes.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2053230X15023869/hv5318sup1.pdf |
PDB reference: methionine γ-lyase, 5dx5