4MKJ

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

4MKJ の概要

• エントリーDOI: 10.2210/pdb4mkj/pdb
• 関連するPDBエントリー: 2RFV 4MKK
• 分子名称: Methionine gamma-lyase, PENTAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: pyridoxal-5'-phosphate, plp-dependent enzyme, lyase, aminotransferase class-v, allicine
• 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: 43942.92

構造登録者

Revtovich, S.V.,Nikulin, A.D.,Morozova, E.A.,Zakomirdina, L.N.,Demidkina, T.V. (登録日: 2013-09-05, 公開日: 2014-11-12, 最終更新日: 2023-12-06)

主引用文献

Morozova, E.A.,Revtovich, S.V.,Anufrieva, N.V.,Kulikova, V.V.,Nikulin, A.D.,Demidkina, T.V.
Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme.
Acta Crystallogr.,Sect.D, 70:3034-3042, 2014

PubMed Abstract: The interaction of Citrobacter freundii methionine γ-lyase (MGL) and the mutant form in which Cys115 is replaced by Ala (MGL C115A) with the nonprotein amino acid (2R)-2-amino-3-[(S)-prop-2-enylsulfinyl]propanoic acid (alliin) was investigated. It was found that MGL catalyzes the β-elimination reaction of alliin to form 2-propenethiosulfinate (allicin), pyruvate and ammonia. The β-elimination reaction of alliin is followed by the inactivation and modification of SH groups of the wild-type and mutant enzymes. Three-dimensional structures of inactivated wild-type MGL (iMGL wild type) and a C115A mutant form (iMGL C115A) were determined at 1.85 and 1.45 Å resolution and allowed the identification of the SH groups that were oxidized by allicin. On this basis, the mechanism of the inactivation of MGL by alliin, a new suicide substrate of MGL, is proposed.

PubMed: 25372692
DOI: 10.1107/S1399004714020938

実験手法

X-RAY DIFFRACTION (1.849 Å)