|
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 |
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