1w1n

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[[Image:1w1n.png|left|200px]]
 
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{{STRUCTURE_1w1n| PDB=1w1n | SCENE= }}
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==The solution structure of the FATC Domain of the Protein Kinase TOR1 from yeast==
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<StructureSection load='1w1n' size='340' side='right'caption='[[1w1n]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1w1n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W1N 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">Solution NMR, 20 models</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=1w1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w1n OCA], [https://pdbe.org/1w1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w1n RCSB], [https://www.ebi.ac.uk/pdbsum/1w1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w1n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TOR1_YEAST TOR1_YEAST] Phosphatidylinositol 3-kinase homolog, 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. TORC1 controls many of these processes via TIP41-TAP42-mediated inhibition of the type 2A-related phosphatases PP2A and SIT4.<ref>PMID:7606777</ref> <ref>PMID:8741837</ref> <ref>PMID:9843498</ref> <ref>PMID:9539725</ref> <ref>PMID:10329624</ref> <ref>PMID:10198052</ref> <ref>PMID:10604478</ref> <ref>PMID:10995454</ref> <ref>PMID:11741537</ref> <ref>PMID:15620355</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w1/1w1n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w1n ConSurf].
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<div style="clear:both"></div>
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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 highly conserved Ser/Thr kinase that plays a central role in the control of cellular growth. TOR has a characteristic multidomain structure. Only the kinase domain has catalytic function; the other domains are assumed to mediate interactions with TOR substrates and regulators. Except for the rapamycin-binding domain, there are no high-resolution structural data available for TOR. Here, we present a structural, biophysical, and mutagenesis study of the extremely conserved COOH-terminal FATC domain. The importance of this domain for TOR function has been highlighted in several publications. We show that the FATC domain, in its oxidized form, exhibits a novel structural motif consisting of an alpha-helix and a COOH-terminal disulfide-bonded loop between two completely conserved cysteine residues. Upon reduction, the flexibility of the loop region increases dramatically. The structural data, the redox potential of the disulfide bridge, and the biochemical data of a cysteine to serine mutant indicate that the intracellular redox potential can affect the cellular amount of the TOR protein via the FATC domain. Because the amount of TOR mRNA is not changed, the redox state of the FATC disulfide bond is probably influencing the degradation of TOR.
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===THE SOLUTION STRUCTURE OF THE FATC DOMAIN OF THE PROTEIN KINASE TOR1 FROM YEAST===
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The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability.,Dames SA, Mulet JM, Rathgeb-Szabo K, Hall MN, Grzesiek S J Biol Chem. 2005 May 27;280(21):20558-64. Epub 2005 Mar 16. PMID:15772072<ref>PMID:15772072</ref>
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{{ABSTRACT_PUBMED_15772072}}
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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 1w1n" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[1w1n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W1N OCA].
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015772072</ref><references group="xtra"/>
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__TOC__
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[[Category: Phosphatidylinositol 3-kinase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Dames, S A.]]
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[[Category: Dames SA]]
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[[Category: Grzesiek, S.]]
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[[Category: Grzesiek S]]
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[[Category: Hall, M N.]]
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[[Category: Hall MN]]
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[[Category: Mulet, J M.]]
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[[Category: Mulet JM]]
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[[Category: Rathgeb-Szabo, K.]]
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[[Category: Rathgeb-Szabo K]]
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[[Category: Disulfide bond]]
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[[Category: Redox-regulation]]
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[[Category: Ser/thr kinase]]
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[[Category: Target of rapamycin]]
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[[Category: Tor]]
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[[Category: Transferase]]
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Current revision

The solution structure of the FATC Domain of the Protein Kinase TOR1 from yeast

PDB ID 1w1n

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