3FGP

2.05 a Crystal Structure of CysM from Mycobacterium Tuberculosis - Open and Closed Conformations

3FGP の概要

• エントリーDOI: 10.2210/pdb3fgp/pdb
• 関連するPDBエントリー: 3DKI
• 分子名称: Cysteine synthase B (2 entities in total)
• 機能のキーワード: cysteine synthase, cysm, tuberculosis, cyso, o-phosphoserine, amino-acid biosynthesis, cysteine biosynthesis, pyridoxal phosphate, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69904.47

構造登録者

Agren, D.,Schnell, R.,Schneider, G. (登録日: 2008-12-08, 公開日: 2008-12-23, 最終更新日: 2023-11-22)

主引用文献

Agren, D.,Schnell, R.,Schneider, G.
The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity
Febs Lett., 583:330-336, 2009

PubMed Abstract: A new crystal structure of the dimeric cysteine synthase CysM from Mycobacterium tuberculosis reveals an open and a closed conformation of the enzyme. In the closed conformation the five carboxy-terminal amino acid residues are inserted into the active site cleft. Removal of this segment results in a decreased lifetime of the alpha-aminoacrylate reaction intermediate, an increased sensitivity to oxidants such as hydrogen peroxide, and loss of substrate selectivity with respect to the sulfur carrier thiocarboxylated CysO. These results highlight features of CysM that might be of particular importance for cysteine biosynthesis under oxidative stress in M. tuberculosis.

PubMed: 19101553
DOI: 10.1016/j.febslet.2008.12.019

実験手法

X-RAY DIFFRACTION (2.05 Å)