5M3Z

Crystal structure of Citrobacter freundii methionine gamma-lyase with C115H replacement in the complex with L-norleucine

5M3Z の概要

• エントリーDOI: 10.2210/pdb5m3z/pdb
• 分子名称: Methionine gamma-lyase, PYRIDOXAL-5'-PHOSPHATE, NORLEUCINE, ... (6 entities in total)
• 機能のキーワード: methionine gamma-lyase, c115h substitution, l-norleucine, 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: 43878.61

構造登録者

Revtovich, S.V.,Nikulin, A.D.,Anufrieva, N.V.,Morozova, E.A.,Demidkina, T.V. (登録日: 2016-10-17, 公開日: 2017-06-28, 最終更新日: 2024-01-17)

主引用文献

Revtovich, S.V.,Morozova, E.A.,Kulikova, V.V.,Anufrieva, N.V.,Osipova, T.I.,Koval, V.S.,Nikulin, A.D.,Demidkina, T.V.
Crystal structure of mutant form Cys115His of Citrobacter freundii methionine gamma-lyase complexed with l-norleucine.
Biochim. Biophys. Acta, 1865:1123-1128, 2017

PubMed Abstract: The mutant form of Citrobacter freundii methionine γ-lyase with the replacement of active site Cys115 for His has been found to be inactive in the γ-elimination reaction of methionine while fully active in the γ-elimination reaction of O-acetyl-l-homoserine and in the β-elimination reaction of S-alk(en)yl-substituted cysteines. In this work, the crystal structure of the mutant enzyme complexed with competitive inhibitor, l-norleucine was determined at 1.45Å resolution. At the enzyme active site the inhibitor proved to be bound both noncovalently and covalently, which corresponds to the two intermediates of the γ- and β-elimination reactions, Michaelis complex and the external aldimine. Analysis of the structure allowed us to suggest the possible reason for the inability of the mutant enzyme to catalyze the physiological reaction.

PubMed: 28602917
DOI: 10.1016/j.bbapap.2017.06.001

実験手法

X-RAY DIFFRACTION (1.45 Å)