1OKT

X-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium falciparum

1OKT の概要

• エントリーDOI: 10.2210/pdb1okt/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE, FORMIC ACID (3 entities in total)
• 機能のキーワード: gst, plasmodium falciparum, transferase
• 由来する生物種: PLASMODIUM FALCIPARUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49864.20

構造登録者

Fritz-Wolf, K.,Becker, A.,Rahlfs, s.,Harwaldt, P.,Schirmer, R.H.,Kabsch, W.,Becker, K. (登録日: 2003-07-29, 公開日: 2003-11-20, 最終更新日: 2024-05-08)

主引用文献

Fritz-Wolf, K.,Becker, A.,Rahlfs, S.,Harwaldt, P.,Schirmer, R.H.,Kabsch, W.,Becker, K.
X-Ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium Falciparum
Proc.Natl.Acad.Sci.USA, 100:13821-, 2003

PubMed Abstract: GSTs catalyze the conjugation of glutathione with a wide variety of hydrophobic compounds, generally resulting in nontoxic products that can be readily eliminated. In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one GST isoenzyme (PfGST). This GST is highly abundant in the parasite, its activity was found to be increased in chloroquine-resistant cells, and it has been shown to act as a ligandin for parasitotoxic hemin. Thus, the enzyme represents a promising target for antimalarial drug development. We now have solved the crystal structure of PfGST at a resolution of 1.9 A. The homodimeric protein of 26 kDa per subunit represents a GST form that cannot be assigned to any of the known GST classes. In comparison to other GSTs, and, in particular, to the human isoforms, PfGST possesses a shorter C-terminal section resulting in a more solvent-accessible binding site for the hydrophobic and amphiphilic substrates. The structure furthermore reveals features in this region that could be exploited for the design of specific PfGST inhibitors.

PubMed: 14623980
DOI: 10.1073/PNAS.2333763100

実験手法

X-RAY DIFFRACTION (1.9 Å)