7PQH

Cryo-EM structure of Saccharomyces cerevisiae TOROID (TORC1 Organized in Inhibited Domains).

これはPDB形式変換不可エントリーです。

7PQH の概要

• エントリーDOI: 10.2210/pdb7pqh/pdb
• EMDBエントリー: 13594 13595
• 分子名称: Target of rapamycin complex 1 subunit KOG1,Target of rapamycin complex 1 subunit Kog1, Target of rapamycin complex subunit LST8, Serine/threonine-protein kinase TOR2 (3 entities in total)
• 機能のキーワード: target of rapamycin, torc1, kog1, lst8, tor2, frb domain, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 1998351.52

構造登録者

Felix, J.,Prouteau, M.,Bourgoint, C.,Bonadei, L.,Desfosses, A.,Gabus, C.,Sadian, Y.,Savvides, S.N.,Gutsche, I.,Loewith, R. (登録日: 2021-09-17, 公開日: 2023-01-18, 最終更新日: 2024-10-23)

主引用文献

Prouteau, M.,Bourgoint, C.,Felix, J.,Bonadei, L.,Sadian, Y.,Gabus, C.,Savvides, S.N.,Gutsche, I.,Desfosses, A.,Loewith, R.
EGOC inhibits TOROID polymerization by structurally activating TORC1.
Nat.Struct.Mol.Biol., 30:273-285, 2023

PubMed Abstract: Target of rapamycin complex 1 (TORC1) is a protein kinase controlling cell homeostasis and growth in response to nutrients and stresses. In Saccharomyces cerevisiae, glucose depletion triggers a redistribution of TORC1 from a dispersed localization over the vacuole surface into a large, inactive condensate called TOROID (TORC1 organized in inhibited domains). However, the mechanisms governing this transition have been unclear. Here, we show that acute depletion and repletion of EGO complex (EGOC) activity is sufficient to control TOROID distribution, independently of other nutrient-signaling pathways. The 3.9-Å-resolution structure of TORC1 from TOROID cryo-EM data together with interrogation of key interactions in vivo provide structural insights into TORC1-TORC1' and TORC1-EGOC interaction interfaces. These data support a model in which glucose-dependent activation of EGOC triggers binding to TORC1 at an interface required for TOROID assembly, preventing TORC1 polymerization and promoting release of active TORC1.

PubMed: 36702972
DOI: 10.1038/s41594-022-00912-6

実験手法

ELECTRON MICROSCOPY (3.87 Å)