5fvm: Difference between revisions
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==Cryo electron microscopy of a complex of Tor and Lst8== | ==Cryo electron microscopy of a complex of Tor and Lst8== | ||
<StructureSection load='5fvm' size='340' side='right' caption='[[5fvm]], [[Resolution|resolution]] 6.70Å' scene=''> | <StructureSection load='5fvm' size='340' side='right'caption='[[5fvm]], [[Resolution|resolution]] 6.70Å' scene=''> | ||
== Structural highlights == | == 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> | <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://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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvm ProSAT]</span></td></tr> | </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> | ||
<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], [http://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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</div> | </div> | ||
<div class="pdbe-citations 5fvm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5fvm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Serine/threonine protein kinase|Serine/threonine protein kinase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cbs 712]] | |||
[[Category: Large Structures]] | |||
[[Category: Baretic, D]] | [[Category: Baretic, D]] | ||
[[Category: Berndt, A]] | [[Category: Berndt, A]] | ||
Revision as of 10:36, 23 October 2019
Cryo electron microscopy of a complex of Tor and Lst8Cryo electron microscopy of a complex of Tor and Lst8
Structural highlights
Publication Abstract from PubMedThe 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 AlsoReferences
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