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| | <SX load='5fvm' size='340' side='right' viewer='molstar' caption='[[5fvm]], [[Resolution|resolution]] 6.70Å' scene=''> | | <SX load='5fvm' size='340' side='right' viewer='molstar' caption='[[5fvm]], [[Resolution|resolution]] 6.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fvm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_712 Cbs 712]. 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://proteopedia.org/fgij/fg.htm?mol=5FVM FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KMAR_30040 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4911 CBS 712]), KMAR_20458 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4911 CBS 712])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvm ProSAT]</span></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> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Cbs 712]] | + | [[Category: Kluyveromyces marxianus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baretic, D]] | + | [[Category: Baretic D]] |
| - | [[Category: Berndt, A]] | + | [[Category: Berndt A]] |
| - | [[Category: Johnson, C M]] | + | [[Category: Johnson CM]] |
| - | [[Category: Ohashi, Y]] | + | [[Category: Ohashi Y]] |
| - | [[Category: Williams, R L]] | + | [[Category: Williams RL]] |
| - | [[Category: Cryo-em]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Lst8]]
| + | |
| - | [[Category: Mtor]]
| + | |
| - | [[Category: Mtorc1]]
| + | |
| - | [[Category: Pikk]]
| + | |
| - | [[Category: S/t protein kinase]]
| + | |
| - | [[Category: Tor]]
| + | |
| - | [[Category: Torc1]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Baretic D, Berndt A, Ohashi Y, Johnson CM, Williams RL. Tor forms a dimer through an N-terminal helical solenoid with a complex topology. Nat Commun. 2016 Apr 13;7:11016. doi: 10.1038/ncomms11016. PMID:27072897 doi:http://dx.doi.org/10.1038/ncomms11016
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