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5fvm

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(New page: '''Unreleased structure''' The entry 5fvm is ON HOLD Authors: Baretic, D., Berndt, A., Ohashi, Y., Johnson, C.M., Williams, R.L. Description: Cryo electron microscopy of a complex of T...)
Current revision (13:28, 26 July 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5fvm is ON HOLD
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==Cryo electron microscopy of a complex of Tor and Lst8==
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<SX load='5fvm' size='340' side='right' viewer='molstar' caption='[[5fvm]], [[Resolution|resolution]] 6.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Baretic, D., Berndt, A., Ohashi, Y., Johnson, C.M., Williams, R.L.
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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>
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Description: Cryo electron microscopy of a complex of Tor and Lst8
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Williams, R.L]]
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<div class="pdbe-citations 5fvm" style="background-color:#fffaf0;"></div>
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[[Category: Baretic, D]]
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[[Category: Johnson, C.M]]
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==See Also==
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[[Category: Berndt, A]]
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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[[Category: Ohashi, Y]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Kluyveromyces marxianus]]
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[[Category: Large Structures]]
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[[Category: Baretic D]]
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[[Category: Berndt A]]
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[[Category: Johnson CM]]
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[[Category: Ohashi Y]]
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[[Category: Williams RL]]

Current revision

Cryo electron microscopy of a complex of Tor and Lst8

5fvm, resolution 6.70Å

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