+Search query
-Structure paper
Title | Tor forms a dimer through an N-terminal helical solenoid with a complex topology. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 7, Page 11016, Year 2016 |
Publish date | Apr 13, 2016 |
Authors | Domagoj Baretić / Alex Berndt / Yohei Ohashi / Christopher M Johnson / Roger L Williams / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:27072897 / PubMed Central |
Methods | EM (single particle) |
Resolution | 6.1 - 10.5 Å |
Structure data | EMDB-3329, PDB-5fvm: EMDB-3334: EMDB-3335: EMDB-3336: |
Source |
|
Keywords | TRANSFERASE / CRYO-EM / TOR / LST8 / MTOR / KINASE / PIKK / S/T PROTEIN KINASE / TORC1 / MTORC1 |