type	Journal Article
authors	Revtovich S, Anufrieva N, Morozova E, Kulikova V, Nikulin A, Demidkina T
title	Structure of methionine γ-lyase from Clostridium sporogenes
journal	Acta Crystallograph Sect F Struct Biol Cryst Commun.
Activity	4.4.1.11
sel	selected
ui	26750487
year	(2016)
volume	72
number	1
pages	65-71
keywords	Clostridium sporogenes; active site; methionine γ-lyase; pyridoxal 5′-phosphate-binding site; tetrameric contacts
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.
last changed	2017/10/02 10:04