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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 DOI10.2210/pdb7pqh/pdb
EMDB information13594 13595
DescriptorTarget 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 Keywordstarget of rapamycin, torc1, kog1, lst8, tor2, frb domain, signaling protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains12
Total formula weight1998351.52
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 citationProuteau, 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: 36702972
DOI: 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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