5fvm: Difference between revisions
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The | ==Cryo electron microscopy of a complex of Tor and Lst8== | ||
<StructureSection load='5fvm' size='340' side='right' caption='[[5fvm]], [[Resolution|resolution]] 6.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fvm]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FVM FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvm OCA], [http://pdbe.org/5fvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvm RCSB], [http://www.ebi.ac.uk/pdbsum/5fvm PDBsum]</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5fvm" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Baretic, D]] | [[Category: Baretic, D]] | ||
[[Category: Berndt, A]] | [[Category: Berndt, A]] | ||
[[Category: Johnson, C M]] | |||
[[Category: Ohashi, Y]] | [[Category: Ohashi, Y]] | ||
[[Category: Williams, R L]] | |||
[[Category: Cryo-em]] | |||
[[Category: Kinase]] | |||
[[Category: Lst8]] | |||
[[Category: Mtor]] | |||
[[Category: Mtorc1]] | |||
[[Category: Pikk]] | |||
[[Category: S/t protein kinase]] | |||
[[Category: Tor]] | |||
[[Category: Torc1]] | |||
[[Category: Transferase]] | |||
