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Structure of methionine ?-lyase from Clostridium sporogenes.


ABSTRACT: Methionine ?-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the ?-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.

SUBMITTER: Revtovich S 

PROVIDER: S-EPMC4708053 | BioStudies | 2016-01-01

REPOSITORIES: biostudies

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