1mt6: Difference between revisions

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OCA

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-[[Image:1mt6.gif|left|200px]]<br />
-<applet load="1mt6" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1mt6, resolution 2.20&Aring;" />
-'''Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy'''<br />
-==Overview==
+==Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy==
-The SET domain contains the catalytic center of lysine methyltransferases, that target the N-terminal tails of histones and regulate chromatin, function. Here we report the structure of the SET7/9 protein in the, absence and presence of its cofactor product, S-adenosyl-L-homocysteine, (AdoHcy). A knot within the SET domain helps form the methyltransferase, active site, where AdoHcy binds and lysine methylation is likely to occur., A structure-guided comparison of sequences within the SET protein family, suggests that the knot substructure and active site environment are, conserved features of the SET domain.
+<StructureSection load='1mt6' size='340' side='right'caption='[[1mt6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1mt6]] is a 1 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=1MT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MT6 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]] 2.2&#8491;</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=1mt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt6 OCA], [https://pdbe.org/1mt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1mt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mt6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== 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/mt/1mt6_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=1mt6 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-MT6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MT6 OCA].
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-The active site of the SET domain is constructed on a knot., Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S, Nat Struct Biol. 2002 Nov;9(11):833-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12389038 12389038]
+__TOC__
-[[Category: Histone-lysine N-methyltransferase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Devarakonda, S.]]
+[[Category: Devarakonda S]]
-[[Category: Harp, J.M.]]
+[[Category: Harp JM]]
-[[Category: Jacobs, S.A.]]
+[[Category: Jacobs SA]]
-[[Category: Khorasanizadeh, S.]]
+[[Category: Khorasanizadeh S]]
-[[Category: Kim, Y.]]
+[[Category: Kim Y]]
-[[Category: Rastinejad, F.]]
+[[Category: Rastinejad F]]
-[[Category: SAH]]
-[[Category: adohcy]]
-[[Category: histone lysine methyltransferase]]
-[[Category: knot]]
-[[Category: set domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:14:51 2007''