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'''Unreleased structure'''


The entry 5fvm is ON HOLD
==Cryo electron microscopy of a complex of Tor and Lst8==
<SX load='5fvm' size='340' side='right' viewer='molstar' caption='[[5fvm]], [[Resolution|resolution]] 6.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fvm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_marxianus Kluyveromyces marxianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FVM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvm OCA], [https://pdbe.org/5fvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fvm RCSB], [https://www.ebi.ac.uk/pdbsum/5fvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvm ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 alpha-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.


Authors: 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.,Baretic D, Berndt A, Ohashi Y, Johnson CM, Williams RL Nat Commun. 2016 Apr 13;7:11016. doi: 10.1038/ncomms11016. PMID:27072897<ref>PMID:27072897</ref>


Description: Cryo electron microscopy of a complex of Tor and Lst8
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Williams, R.L]]
<div class="pdbe-citations 5fvm" style="background-color:#fffaf0;"></div>
[[Category: Baretic, D]]
 
[[Category: Johnson, C.M]]
==See Also==
[[Category: Berndt, A]]
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
[[Category: Ohashi, Y]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Kluyveromyces marxianus]]
[[Category: Large Structures]]
[[Category: Baretic D]]
[[Category: Berndt A]]
[[Category: Johnson CM]]
[[Category: Ohashi Y]]
[[Category: Williams RL]]
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