1xqh

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[[Image:1xqh.png|left|200px]]
 
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{{STRUCTURE_1xqh| PDB=1xqh | SCENE= }}
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==Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH==
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<StructureSection load='1xqh' size='340' side='right'caption='[[1xqh]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xqh]] is a 4 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=1XQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XQH 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">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=1xqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqh OCA], [https://pdbe.org/1xqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xqh RCSB], [https://www.ebi.ac.uk/pdbsum/1xqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</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/xq/1xqh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1xqh 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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p53 is a tumour suppressor that regulates the cellular response to genotoxic stresses. p53 is a short-lived protein and its activity is regulated mostly by stabilization via different post-translational modifications. Here we report a novel mechanism of p53 regulation through lysine methylation by Set9 methyltransferase. Set9 specifically methylates p53 at one residue within the carboxyl-terminus regulatory region. Methylated p53 is restricted to the nucleus and the modification positively affects its stability. Set9 regulates the expression of p53 target genes in a manner dependent on the p53-methylation site. The crystal structure of a ternary complex of Set9 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of p53 by this lysine methyltransferase.
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===Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH===
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Regulation of p53 activity through lysine methylation.,Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D Nature. 2004 Nov 18;432(7015):353-60. Epub 2004 Nov 3. PMID:15525938<ref>PMID:15525938</ref>
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{{ABSTRACT_PUBMED_15525938}}
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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 1xqh" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[1xqh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQH OCA].
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 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:015525938</ref><references group="xtra"/>
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__TOC__
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[[Category: Histone-lysine N-methyltransferase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Barlev, N A.]]
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[[Category: Large Structures]]
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[[Category: Chuikov, S.]]
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[[Category: Barlev NA]]
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[[Category: Gamblin, S J.]]
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[[Category: Chuikov S]]
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[[Category: Ivanov, G S.]]
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[[Category: Gamblin SJ]]
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[[Category: Justin, N.]]
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[[Category: Ivanov GS]]
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[[Category: Kurash, J K.]]
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[[Category: Justin N]]
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[[Category: McKinney, K.]]
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[[Category: Kurash JK]]
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[[Category: Prives, C.]]
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[[Category: McKinney K]]
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[[Category: Reinberg, D.]]
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[[Category: Prives C]]
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[[Category: Tempst, P.]]
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[[Category: Reinberg D]]
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[[Category: Wilson, J R.]]
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[[Category: Tempst P]]
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[[Category: Xiao, B.]]
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[[Category: Wilson JR]]
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[[Category: Lysine methylation]]
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[[Category: Xiao B]]
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[[Category: Set-domain]]
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[[Category: Set9-p53 complex]]
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[[Category: Transferase]]
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Current revision

Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH

PDB ID 1xqh

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