Structural highlights
Publication Abstract from PubMed
Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the gamma-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 A 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.
Structure of methionine gamma-lyase from Clostridium sporogenes.,Revtovich S, Anufrieva N, Morozova E, Kulikova V, Nikulin A, Demidkina T Acta Crystallogr F Struct Biol Commun. 2016 Jan 1;72(Pt 1):65-71. doi:, 10.1107/S2053230X15023869. Epub 2016 Jan 1. PMID:26750487[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Revtovich S, Anufrieva N, Morozova E, Kulikova V, Nikulin A, Demidkina T. Structure of methionine gamma-lyase from Clostridium sporogenes. Acta Crystallogr F Struct Biol Commun. 2016 Jan 1;72(Pt 1):65-71. doi:, 10.1107/S2053230X15023869. Epub 2016 Jan 1. PMID:26750487 doi:http://dx.doi.org/10.1107/S2053230X15023869
