2RFV

High resolution structure of L-methionine gamma-lyase from Citrobacter freundii

2RFV の概要

• エントリーDOI: 10.2210/pdb2rfv/pdb
• 関連するPDBエントリー: 1Y4I
• 分子名称: Methionine gamma-lyase, CHLORIDE ION (3 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: 43286.49

構造登録者

Nikulin, A.D.,Revtovich, S.V.,Morozova, E.A.,Nevskaya, N.A.,Nikonov, S.V.,Garber, M.B.,Demidkina, T.V. (登録日: 2007-10-02, 公開日: 2008-08-19, 最終更新日: 2023-11-15)

主引用文献

Nikulin, A.,Revtovich, S.,Morozova, E.,Nevskaya, N.,Nikonov, S.,Garber, M.,Demidkina, T.
High-resolution structure of methionine gamma-lyase from Citrobacter freundii.
Acta Crystallogr.,Sect.D, 64:211-218, 2008

PubMed Abstract: Pyridoxal 5'-phosphate-dependent methionine gamma-lyase (MGL) is involved in the metabolism of sulfur-containing amino acids. The enzyme is a promising target in some anaerobic pathogens and is effective in cancer-cell treatment. The structure of the MGL holoenzyme from Citrobacter freundii has previously been determined at 1.9 A resolution. By modification of the crystallization procedure, the previously determined structure of C. freundii MGL has been improved to 1.35 A resolution with R and R(free) values of 0.152 and 0.177, respectively. This high-resolution structure makes it possible to analyze the interactions between the monomers in detail and to reveal the structurally invariant regions that are responsible for monomer-monomer recognition during the formation of the active enzyme. Details of the mode of cofactor binding and of the flexible regions that may be involved in substrate recognition and binding are also described.

PubMed: 18219122
DOI: 10.1107/S0907444907065390

実験手法

X-RAY DIFFRACTION (1.355 Å)