7ZHX

Leishmania donovani Glucose 6-Phosphate Dehydrogenase (N-terminal deletion variant)complexed with NADP(H)

7ZHX の概要

• エントリーDOI: 10.2210/pdb7zhx/pdb
• 関連するPDBエントリー: 7ZHT 7ZHU 7ZHV 7ZHW 7ZHY 7ZHZ
• 分子名称: Glucose-6-phosphate 1-dehydrogenase, DI(HYDROXYETHYL)ETHER, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: trypanosoma, leishmania donovani, glucose 6-phosphate dehydrogenase, g6p, nadp(h), pentose phosphate pathway, oxidoreductase
• 由来する生物種: Leishmania donovani
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58317.85

構造登録者

Fritz-Wolf, K.,Berneburg, I. (登録日: 2022-04-07, 公開日: 2022-12-14, 最終更新日: 2024-05-01)

主引用文献

Berneburg, I.,Rahlfs, S.,Becker, K.,Fritz-Wolf, K.
Crystal structure of Leishmania donovani glucose 6-phosphate dehydrogenase reveals a unique N-terminal domain.
Commun Biol, 5:1353-1353, 2022

PubMed Abstract: Since unicellular parasites highly depend on NADPH as a source for reducing equivalents, the pentose phosphate pathway, especially the first and rate-limiting NADPH-producing enzyme glucose 6-phosphate dehydrogenase (G6PD), is considered an excellent antitrypanosomatid drug target. Here we present the crystal structure of Leishmania donovani G6PD (LdG6PD) elucidating the unique N-terminal domain of Kinetoplastida G6PDs. Our investigations on the function of the N-domain suggest its involvement in the formation of a tetramer that is completely different from related Trypanosoma G6PDs. Structural and functional investigations further provide interesting insights into the binding mode of LdG6PD, following an ordered mechanism, which is confirmed by a G6P-induced domain shift and rotation of the helical N-domain. Taken together, these insights into LdG6PD contribute to the understanding of G6PDs' molecular mechanisms and provide an excellent basis for further drug discovery approaches.

PubMed: 36494598
DOI: 10.1038/s42003-022-04307-7

実験手法

X-RAY DIFFRACTION (1.9 Å)