3JWA

Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with methionine phosphinate

3JWA の概要

• エントリーDOI: 10.2210/pdb3jwa/pdb
• 関連するPDBエントリー: 1E5E 1UKJ 1Y4I 2O7C 2RFV 3JW9 3JWB
• 分子名称: Methionine gamma-lyase, (1-AMINO-3-METHYLSULFANYL-PROPYL)-PHOSPHINIC ACID, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: pyridoxal-5'-phosphate, plp-dependent enzyme, 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: 43880.70

構造登録者

Revtovish, S.V.,Nikulin, A.D.,Morozova, E.A.,Demidkina, T.V. (登録日: 2009-09-18, 公開日: 2010-09-08, 最終更新日: 2023-11-22)

主引用文献

Revtovich, S.V.,Morozova, E.A.,Khurs, E.N.,Zakomirdina, L.N.,Nikulin, A.D.,Demidkina, T.V.,Khomutov, R.M.
Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates.
Biochemistry Mosc., 76:564-570, 2011

PubMed Abstract: Crystal structures of Citrobacter freundii methionine γ-lyase complexes with the substrates of γ- (L-1-amino-3-methylthiopropylphosphinic acid) and β- (S-ethyl-L-cysteine) elimination reactions and the competitive inhibitor L-norleucine have been determined at 1.45, 1.8, and 1.63 Å resolution, respectively. All three amino acids occupy the active site of the enzyme but do not form a covalent bond with pyridoxal 5'-phosphate. Hydrophobic interactions between the active site residues and the side groups of the substrates and the inhibitor are supposed to cause noncovalent binding. Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrates and the inhibitor. The hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acids.

PubMed: 21639836
DOI: 10.1134/S0006297911050063

実験手法

X-RAY DIFFRACTION (1.45 Å)