1DGM

CRYSTAL STRUCTURE OF ADENOSINE KINASE FROM TOXOPLASMA GONDII

1DGM の概要

• エントリーDOI: 10.2210/pdb1dgm/pdb
• 分子名称: ADENOSINE KINASE, MAGNESIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: toxoplasma gondii, adenosine kinase, purine metabolism, transferase
• 由来する生物種: Toxoplasma gondii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38811.88

構造登録者

Cook, W.J.,DeLucas, L.J.,Chattopadhyay, D. (登録日: 1999-11-24, 公開日: 2000-11-29, 最終更新日: 2024-11-13)

主引用文献

Cook, W.J.,DeLucas, L.J.,Chattopadhyay, D.
Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution.
Protein Sci., 9:704-707, 2000

PubMed Abstract: Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme.

PubMed: 10794412

実験手法

X-RAY DIFFRACTION (1.8 Å)