title: Structure of methionine γ-lyase from Clostridium sporogenes.
abstract: 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.
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
authors.forename: Svetlana
authors.initials: S
authors.lastname: Revtovich
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
authors.forename: Natalya
authors.initials: N
authors.lastname: Anufrieva
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
authors.forename: Elena
authors.initials: E
authors.lastname: Morozova
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
authors.forename: Vitalia
authors.initials: V
authors.lastname: Kulikova
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
authors.forename: Alexey
authors.initials: A
authors.lastname: Nikulin
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 119991, Russian Federation.
authors.forename: Tatyana
authors.initials: T
authors.lastname: Demidkina
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D013437:Carbon-Sulfur Lyases / Q000737:chemistry*; D020134:Catalytic Domain; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D007700:Kinetics; D008715:Methionine / Q000737:chemistry; D008958:Models, Molecular; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D011732:Pyridoxal Phosphate / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D011732:Pyridoxal Phosphate; D008715:Methionine; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase
keywords: Clostridium sporogenes; active site; methionine γ-lyase; pyridoxal 5′-phosphate-binding site; tetrameric contacts