2O2C

Crystal structure of phosphoglucose isomerase from T. brucei containing glucose-6-phosphate in the active site

2O2C の概要

• エントリーDOI: 10.2210/pdb2o2c/pdb
• 関連するPDBエントリー: 2O2D
• 分子名称: Glucose-6-phosphate isomerase, glycosomal, GLUCOSE-6-PHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: dimer, isomerase
• 由来する生物種: Trypanosoma brucei brucei
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 206708.94

構造登録者

Arsenieva, D.,Mazock, G.H.,Appavu, B.L.,Jeffery, C.J. (登録日: 2006-11-29, 公開日: 2007-11-13, 最終更新日: 2023-08-30)

主引用文献

Arsenieva, D.,Appavu, B.L.,Mazock, G.H.,Jeffery, C.J.
Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with glucose-6-phosphate at 1.6 A resolution
Proteins, 74:72-80, 2008

PubMed Abstract: Enzymes of glycolysis in Trypanosoma brucei have been identified as potential drug targets for African sleeping sickness because glycolysis is the only source of ATP for the bloodstream form of this parasite. Several inhibitors were previously reported to bind preferentially to trypanosomal phosphoglucose isomerase (PGI, the second enzyme in glycolysis) than to mammalian PGIs, which suggests that PGI might make a good target for species-specific drug design. Herein, we report recombinant expression, purification, crystallization and X-ray crystal structure determination of T. brucei PGI. One structure solved at 1.6 A resolution contains a substrate, D-glucose-6-phosphate, in an extended conformation in the active site. A second structure solved at 1.9 A resolution contains a citrate molecule in the active site. The structures are compared with the crystal structures of PGI from humans and from Leishmania mexicana. The availability of recombinant tPGI and its first high-resolution crystal structures are initial steps in considering this enzyme as a potential drug target.

PubMed: 18561188
DOI: 10.1002/prot.22133

実験手法

X-RAY DIFFRACTION (1.58 Å)