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2zfu
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2zfu is ON HOLD until Paper Publication Authors: Murayama, A., Ohmori, K., Fujimura, A., Minami, H., Tanaka, K.Y., Kuroda, T., Oie, S., Daitoku, H.,...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the methyltransferase-like domain of nucleomethylin== | |
| - | + | <StructureSection load='2zfu' size='340' side='right'caption='[[2zfu]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2zfu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZFU FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=2zfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zfu OCA], [https://pdbe.org/2zfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zfu RCSB], [https://www.ebi.ac.uk/pdbsum/2zfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zfu ProSAT]</span></td></tr> | |
| - | + | </table> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RRP8_HUMAN RRP8_HUMAN] Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown.<ref>PMID:18485871</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zf/2zfu_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2zfu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hashimoto H]] | ||
| + | [[Category: Minami H]] | ||
| + | [[Category: Murayama A]] | ||
| + | [[Category: Sato M]] | ||
| + | [[Category: Shimizu T]] | ||
| + | [[Category: Yanagisawa J]] | ||
Current revision
Structure of the methyltransferase-like domain of nucleomethylin
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