6S0C

Crystal structure of methionine gamma-lyase from Citrobacter freundii modified by dimethylthiosulfinate

6S0C の概要

• エントリーDOI: 10.2210/pdb6s0c/pdb
• 関連するPDBエントリー: 2RFV
• 分子名称: Cystathionine gamma-synthase, TRIETHYLENE GLYCOL, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: methionine gamma-lyase, lyase
• 由来する生物種: Citrobacter freundii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43472.39

構造登録者

Revtovich, S.V.,Morozova, E.A.,Nikulin, A.D.,Demidkina, T.V. (登録日: 2019-06-14, 公開日: 2020-04-22, 最終更新日: 2024-01-24)

主引用文献

Revtovich, S.,Morozova, E.,Kulikova, V.,Koval, V.,Anufrieva, N.,Nikulin, A.,Demidkina, T.
Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine gamma-lyase. Structural bases of the enzyme inactivation.
Biochimie, 168:190-197, 2020

PubMed Abstract: Interactions of Citrobacter freundii methionine γ-lyase (MGL) with sulfoxides of typical substrates were investigated. It was found that sulfoxides are suicide substrates of the enzyme. The products of the β- and γ-elimination reactions of sulfoxides, thiosulfinates, oxidize three cysteine residues of the enzyme. Three-dimensional structures of MGL inactivated by dimethyl thiosulfinate and diethyl thiosulfinate were determined at 1.46 Å and 1.59 Å resolution. Analysis of the structures identified SH groups oxidized by thiosulfinates and revealed the structural bases of MGL inactivation. The extent of inactivation of MGL in the catalysis of the β-elimination reaction depends on the length of the «tail» at oxidized Cys115. Oxidation of Cys115 results in MGL incapable to catalyze the stage of methyl mercaptan elimination of the physiological reaction.

PubMed: 31711941
DOI: 10.1016/j.biochi.2019.11.004

実験手法

X-RAY DIFFRACTION (1.46 Å)