7PQH
Cryo-EM structure of Saccharomyces cerevisiae TOROID (TORC1 Organized in Inhibited Domains).
This is a non-PDB format compatible entry.
Summary for 7PQH
Entry DOI | 10.2210/pdb7pqh/pdb |
EMDB information | 13594 13595 |
Descriptor | 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) |
Functional Keywords | target of rapamycin, torc1, kog1, lst8, tor2, frb domain, signaling protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 12 |
Total formula weight | 1998351.52 |
Authors | Felix, J.,Prouteau, M.,Bourgoint, C.,Bonadei, L.,Desfosses, A.,Gabus, C.,Sadian, Y.,Savvides, S.N.,Gutsche, I.,Loewith, R. (deposition date: 2021-09-17, release date: 2023-01-18, Last modification date: 2024-10-23) |
Primary citation | 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 Cited by 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: 36702972DOI: 10.1038/s41594-022-00912-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.87 Å) |
Structure validation
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