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- Title
Structure of methionine γ-lyase from Clostridium sporogenes.
- Authors
Revtovich, Svetlana; Anufrieva, Natalya; Morozova, Elena; Kulikova, Vitalia; Nikulin, Alexey; Demidkina, Tatyana
- 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.
- Subjects
BACTERIAL protein structure; METHIONINE; CLOSTRIDIUM sporogenes
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2016, Vol 72, Issue 1, p65
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X15023869