title: Structure of Citrobacter freundii L-methionine gamma-lyase.
abstract: L-Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes gamma-elimination of L-methionine. The crystal structure of MGL from Citrobacter freundii has been determined at 1.9 A resolution. The spatial fold of the protein is similar to those of MGLs from Pseudomonas putida and Trichomonas vaginalis. The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops.
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, 119991 Moscow, Russia.
authors.forename: D V
authors.initials: DV
authors.lastname: Mamaeva
authors.forename: E A
authors.initials: EA
authors.lastname: Morozova
authors.forename: A D
authors.initials: AD
authors.lastname: Nikulin
authors.forename: S V
authors.initials: SV
authors.lastname: Revtovich
authors.forename: S V
authors.initials: SV
authors.lastname: Nikonov
authors.forename: M B
authors.initials: MB
authors.lastname: Garber
authors.forename: T V
authors.initials: TV
authors.lastname: Demidkina
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D013437:Carbon-Sulfur Lyases / Q000737:chemistry*; D016971:Citrobacter freundii / Q000201:enzymology*; D018360:Crystallography, X-Ray; D015394:Molecular Structure; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase