Tor forms a dimer through an N-terminal helical solenoid with a complex topology

• DOI: 10.1038/ncomms11016
• Publication Date: 2016-04-13T11:34:18Z
• Authors: Domagoj Baretić; Alex Berndt; Yohei Ohashi; Christopher M. Jo...; Roger L. Williams
• Keywords: Models, Molecular; 0301 basic medicine; Saccharomyces cerevisiae Proteins; Science; TOR Serine-Threonine Kinases; Q; Cryoelectron Microscopy; Mechanistic Target of Rapamycin Complex 2; Saccharomyces cerevisiae; Mechanistic Target of Rapamycin Complex 1; Article; Protein Structure, Secondary; Protein Structure, Tertiary; Kluyveromyces; Mice; 03 medical and health sciences; Catalytic Domain; Multiprotein Complexes; Animals; Humans; Protein Multimerization; Protein Binding

Abstract The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates range anabolic and catabolic processes. Tor present in two complexes, TORC1 TORC2, which the Tor–Lst8 heterodimer forms common sub-complex. We have determined cryo-electron microscopy (EM) structure bound to Lst8. Two heterodimers assemble further into dyad-symmetry dimer mediated by Tor–Tor interactions. first 1,300 residues form HEAT repeat-containing α -solenoid with four distinct segments: highly curved 800-residue N-terminal 'spiral', followed 400-residue low-curvature 'bridge' an extended ‘railing’ running along bridge leading 'cap' links FAT region. This complex topology was verified domain insertions offers new interpretation mTORC1 structure. spiral one TOR interacts another, together joint platform for Regulatory Associated Protein (RAPTOR) regulatory subunit.