6LFG

Cryo-EM structure of the Drosophila CTP synthase product-bound filament

6LFG の概要

• エントリーDOI: 10.2210/pdb6lfg/pdb
• EMDBエントリー: 0876
• 分子名称: CTP synthase (1 entity in total)
• 機能のキーワード: product-bound, filament, ligase
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 504947.84

構造登録者

Ji-long, L.,Xian, Z.,Chen-Jun, G. (登録日: 2019-12-02, 公開日: 2020-03-18, 最終更新日: 2024-03-27)

主引用文献

Zhou, X.,Guo, C.J.,Hu, H.H.,Zhong, J.,Sun, Q.,Liu, D.,Zhou, S.,Chang, C.C.,Liu, J.L.
Drosophila CTP synthase can form distinct substrate- and product-bound filaments.
J Genet Genomics, 46:537-545, 2019

PubMed Abstract: Intracellular compartmentation is a key strategy for the functioning of a cell. In 2010, several studies revealed that the metabolic enzyme CTP synthase (CTPS) can form filamentous structures termed cytoophidia in prokaryotic and eukaryotic cells. However, recent structural studies showed that CTPS only forms inactive product-bound filaments in bacteria while forming active substrate-bound filaments in eukaryotic cells. In this study, using negative staining and cryo-electron microscopy, we demonstrate that Drosophila CTPS, whether in substrate-bound or product-bound form, can form filaments. Our results challenge the previous model and indicate that substrate-bound and product-bound filaments can coexist in the same species. We speculate that the ability to switch between active and inactive cytoophidia in the same cells provides an additional layer of metabolic regulation.

PubMed: 31902586
DOI: 10.1016/j.jgg.2019.11.006

実験手法

ELECTRON MICROSCOPY (9.58 Å)