7pqh

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7pqh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PQH FirstGlance]. <br>
<table><tr><td colspan='2'>[[7pqh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PQH FirstGlance]. <br>
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</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=7pqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pqh OCA], [https://pdbe.org/7pqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pqh RCSB], [https://www.ebi.ac.uk/pdbsum/7pqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pqh ProSAT]</span></td></tr>
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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]] 3.87&#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=7pqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pqh OCA], [https://pdbe.org/7pqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pqh RCSB], [https://www.ebi.ac.uk/pdbsum/7pqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pqh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/KOG1_YEAST KOG1_YEAST] Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. KOG1 may have a role in binding and recruiting substrates of TORC1.<ref>PMID:16394584</ref>
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[https://www.uniprot.org/uniprot/KOG1_YEAST KOG1_YEAST]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Target of rapamycin complex 1 (TORC1) is a protein kinase controlling cell homeostasis and growth in response to nutrients and stresses. In Saccharomyces cerevisiae, glucose depletion triggers a redistribution of TORC1 from a dispersed localization over the vacuole surface into a large, inactive condensate called TOROID (TORC1 organized in inhibited domains). However, the mechanisms governing this transition have been unclear. Here, we show that acute depletion and repletion of EGO complex (EGOC) activity is sufficient to control TOROID distribution, independently of other nutrient-signaling pathways. The 3.9-A-resolution structure of TORC1 from TOROID cryo-EM data together with interrogation of key interactions in vivo provide structural insights into TORC1-TORC1' and TORC1-EGOC interaction interfaces. These data support a model in which glucose-dependent activation of EGOC triggers binding to TORC1 at an interface required for TOROID assembly, preventing TORC1 polymerization and promoting release of active TORC1.
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EGOC inhibits TOROID polymerization by structurally activating TORC1.,Prouteau M, Bourgoint C, Felix J, Bonadei L, Sadian Y, Gabus C, Savvides SN, Gutsche I, Desfosses A, Loewith R Nat Struct Mol Biol. 2023 Mar;30(3):273-285. doi: 10.1038/s41594-022-00912-6. , Epub 2023 Jan 26. PMID:36702972<ref>PMID:36702972</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7pqh" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Current revision

Cryo-EM structure of Saccharomyces cerevisiae TOROID (TORC1 Organized in Inhibited Domains).

PDB ID 7pqh

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