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

Domagoj Baretić, Alex Berndt, Yohei Ohashi, Christopher M. Johnson and Roger L. Williams ()
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Domagoj Baretić: MRC Laboratory of Molecular Biology
Alex Berndt: MRC Laboratory of Molecular Biology
Yohei Ohashi: MRC Laboratory of Molecular Biology
Christopher M. Johnson: MRC Laboratory of Molecular Biology
Roger L. Williams: MRC Laboratory of Molecular Biology

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/ncomms11016

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