3ENZ

Arsenolytic structure of Plasmodium falciparum purine nucleoside phosphorylase with hypoxanthine, ribose and arsenate ion

3ENZ の概要

• エントリーDOI: 10.2210/pdb3enz/pdb
• 分子名称: Purine nucleoside phosphorylase, HYPOXANTHINE, 1,4-anhydro-D-ribitol, ... (7 entities in total)
• 機能のキーワード: transferase, catalytically-relevant arsenolytic-intermediate-state complex, glycosyltransferase
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 171448.38

構造登録者

Chaikuad, A.,Brady, R.L. (登録日: 2008-09-26, 公開日: 2009-08-04, 最終更新日: 2023-09-06)

主引用文献

Chaikuad, A.,Brady, R.L.
Conservation of structure and activity in Plasmodium purine nucleoside phosphorylases.
Bmc Struct.Biol., 9:42-42, 2009

PubMed Abstract: Purine nucleoside phosphorylase (PNP) is central to purine salvage mechanisms in Plasmodium parasites, the causative agents of malaria. Most human malaria results from infection either by Plasmodium falciparum (Pf), the deadliest form of the parasite, or by the widespread Plasmodium vivax (Pv). Whereas the PNP enzyme from Pf has previously been studied in detail, despite the prevalence of Pv little is known about many of the key metabolic enzymes from this parasite, including PvPNP.

PubMed: 19575810
DOI: 10.1186/1472-6807-9-42

実験手法

X-RAY DIFFRACTION (2.03 Å)