7RMO

Yeast CTP Synthase (Ura7) Bundle bound to Products at low pH

これはPDB形式変換不可エントリーです。

7RMO の概要

• エントリーDOI: 10.2210/pdb7rmo/pdb
• EMDBエントリー: 24576
• 分子名称: CTP synthase, CYTIDINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: glutaminase and amino-ligase, protein fibril
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 1774075.49

構造登録者

Hansen, J.M.,Lynch, E.M.,Farrell, D.P.,DiMaio, F.,Quispe, J.,Kollman, J.M. (登録日: 2021-07-27, 公開日: 2021-11-24, 最終更新日: 2024-06-05)

主引用文献

Hansen, J.M.,Horowitz, A.,Lynch, E.M.,Farrell, D.P.,Quispe, J.,DiMaio, F.,Kollman, J.M.
Cryo-EM structures of CTP synthase filaments reveal mechanism of pH-sensitive assembly during budding yeast starvation.
Elife, 10:-, 2021

PubMed Abstract: Many metabolic enzymes self-assemble into micron-scale filaments to organize and regulate metabolism. The appearance of these assemblies often coincides with large metabolic changes as in development, cancer, and stress. Yeast undergo cytoplasmic acidification upon starvation, triggering the assembly of many metabolic enzymes into filaments. However, it is unclear how these filaments assemble at the molecular level and what their role is in the yeast starvation response. CTP Synthase (CTPS) assembles into metabolic filaments across many species. Here, we characterize in vitro polymerization and investigate in vivo consequences of CTPS assembly in yeast. Cryo-EM structures reveal a pH-sensitive assembly mechanism and highly ordered filament bundles that stabilize an inactive state of the enzyme, features unique to yeast CTPS. Disruption of filaments in cells with non-assembly or pH-insensitive mutations decreases growth rate, reflecting the importance of regulated CTPS filament assembly in homeotstasis.

PubMed: 34734801
DOI: 10.7554/eLife.73368

実験手法

ELECTRON MICROSCOPY (7 Å)