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1n6c

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(New page: 200px<br /> <applet load="1n6c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6c, resolution 2.30&Aring;" /> '''Structure of SET7/9...)
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[[Image:1n6c.gif|left|200px]]<br />
 
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<applet load="1n6c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n6c, resolution 2.30&Aring;" />
 
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'''Structure of SET7/9'''<br />
 
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==Overview==
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==Structure of SET7/9==
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The methylation of lysine residues of histones plays a pivotal role in the, regulation of chromatin structure and gene expression. Here, we report two, crystal structures of SET7/9, a histone methyltransferase (HMTase) that, transfers methyl groups to Lys4 of histone H3, in complex with, S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution., The structures reveal an active site consisting of: (i) a binding pocket, between the SET domain and a c-SET helix where an AdoMet molecule in an, unusual conformation binds; (ii) a narrow substrate-specific channel that, only unmethylated lysine residues can access; and (iii) a catalytic, tyrosine residue. The methyl group of AdoMet is directed to the narrow, channel where a substrate lysine enters from the opposite side. We, demonstrate that SET7/9 can transfer two but not three methyl groups to, unmodified Lys4 of H3 without substrate dissociation. The unusual features, of the SET domain-containing HMTase discriminate between the un- and, methylated lysine substrate, and the methylation sites for the histone H3, tail.
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<StructureSection load='1n6c' size='340' side='right'caption='[[1n6c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n6c]] 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=1N6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N6C 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]] 2.3&#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=SAM:S-ADENOSYLMETHIONINE'>SAM</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=1n6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6c OCA], [https://pdbe.org/1n6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n6c RCSB], [https://www.ebi.ac.uk/pdbsum/1n6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6c 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/n6/1n6c_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=1n6c ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1N6C 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 SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N6C 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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Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet., Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y, EMBO J. 2003 Jan 15;22(2):292-303. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12514135 12514135]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chang, J.H.]]
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[[Category: Chang JH]]
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[[Category: Cho, Y.]]
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[[Category: Cho Y]]
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[[Category: Kwon, T.W.]]
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[[Category: Kwon TW]]
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[[Category: SAM]]
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[[Category: protein-ligand complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:18:06 2007''
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Current revision

Structure of SET7/9

PDB ID 1n6c

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