5FVM

Cryo electron microscopy of a complex of Tor and Lst8

Summary for 5FVM

• Entry DOI: 10.2210/pdb5fvm/pdb
• EMDB information: 3329
• Descriptor: SERINE/THREONINE-PROTEIN KINASE TOR2, TARGET OF RAPAMYCIN COMPLEX SUBUNIT LST8 (2 entities in total)
• Functional Keywords: transferase, cryo-em, tor, lst8, mtor, kinase, pikk, s/t protein kinase, torc1, mtorc1
• Biological source: KLUYVEROMYCES MARXIANUS; More
• Total number of polymer chains: 4
• Total formula weight: 626721.22

Authors

Baretic, D.,Berndt, A.,Ohashi, Y.,Johnson, C.M.,Williams, R.L. (deposition date: 2016-02-09, release date: 2016-04-20, Last modification date: 2024-05-08)

Primary citation

Baretic, D.,Berndt, A.,Ohashi, Y.,Johnson, C.M.,Williams, R.L.
Tor Forms a Dimer Through an N-Terminal Helical Solenoid with a Complex Topology
Nat.Commun., 7:11016-, 2016

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 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.

PubMed: 27072897
DOI: 10.1038/NCOMMS11016

Experimental method

ELECTRON MICROSCOPY (6.7 Å)