Tor forms a dimer through an N-terminal helical solenoid with a complex topology.
The target of rapamycin (Tor) is a Ser/Thr protein kinase that regulates a range of anabolic and catabolic processes. Tor is present in two complexes, TORC1 and TORC2, in which the Tor-Lst8 heterodimer forms a common sub-complex. We have determined the cryo-electron microscopy (EM) structure of Tor bound to Lst8. ... Two Tor-Lst8 heterodimers assemble further into a dyad-symmetry dimer mediated by Tor-Tor interactions. The first 1,300 residues of Tor form a HEAT repeat-containing α-solenoid with four distinct segments: a highly curved 800-residue N-terminal 'spiral', followed by a 400-residue low-curvature 'bridge' and an extended 'railing' running along the bridge leading to the 'cap' that links to FAT region. This complex topology was verified by domain insertions and offers a new interpretation of the mTORC1 structure. The spiral of one TOR interacts with the bridge of another, which together form a joint platform for the Regulatory Associated Protein of TOR (RAPTOR) regulatory subunit.
Mesh Terms:
Animals, Catalytic Domain, Cryoelectron Microscopy, Humans, Kluyveromyces, Mice, Models, Molecular, Multiprotein Complexes, Protein Binding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases
Animals, Catalytic Domain, Cryoelectron Microscopy, Humans, Kluyveromyces, Mice, Models, Molecular, Multiprotein Complexes, Protein Binding, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases
Nat Commun
Date: Apr. 13, 2016
PubMed ID: 27072897
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