5DX5

Crystal structure of methionine gamma-lyase from Clostridium sporogenes

5DX5 の概要

• エントリーDOI: 10.2210/pdb5dx5/pdb
• 分子名称: Methionine gamma-lyase, PYRIDOXAL-5'-PHOSPHATE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: methionine gamma-lyase, lyase, clostridium sporogenes
• 由来する生物種: Clostridium sporogenes
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87747.63

構造登録者

Revtovich, S.V.,Nikulin, A.D.,Morozova, E.A.,Anufrieva, N.V.,Demidkina, T.V. (登録日: 2015-09-23, 公開日: 2016-01-13, 最終更新日: 2024-01-10)

主引用文献

Revtovich, S.,Anufrieva, N.,Morozova, E.,Kulikova, V.,Nikulin, A.,Demidkina, T.
Structure of methionine gamma-lyase from Clostridium sporogenes.
Acta Crystallogr.,Sect.F, 72:65-71, 2016

PubMed 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.

PubMed: 26750487
DOI: 10.1107/S2053230X15023869

実験手法

X-RAY DIFFRACTION (2.37 Å)