2g46
From Proteopedia
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| - | {{Large structure}} | ||
| - | {{STRUCTURE_2g46| PDB=2g46 | SCENE= }} | ||
| - | ===structure of vSET in complex with meK27 H3 Pept. and cofactor product SAH=== | ||
| - | {{ABSTRACT_PUBMED_16603186}} | ||
| - | == | + | ==structure of vSET in complex with meK27 H3 Pept. and cofactor product SAH== |
| - | [[2g46]] is a 4 chain structure with sequence from [ | + | <StructureSection load='2g46' size='340' side='right'caption='[[2g46]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2g46]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorella_pbcv-1_virus Chlorella pbcv-1 virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G46 FirstGlance]. <br> | ||
| + | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A612L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10506 Chlorella PBCV-1 virus])</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=2g46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g46 OCA], [https://pdbe.org/2g46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g46 RCSB], [https://www.ebi.ac.uk/pdbsum/2g46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g46 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/g4/2g46_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=2g46 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SET domain lysine methyltransferases are known to catalyze site and state-specific methylation of lysine residues in histones that is fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. Here we report the three-dimensional solution structure of the SET domain histone lysine methyltransferase (vSET) from Paramecium bursaria chlorella virus 1 bound to cofactor S-adenosyl-L-homocysteine and a histone H3 peptide containing mono-methylated lysine 27. The dimeric structure, mimicking an enzyme/cofactor/substrate complex, yields the structural basis of the substrate specificity and methylation multiplicity of the enzyme. Our results from mutagenesis and enzyme kinetics analyses argue that a general base mechanism is less likely for lysine methylation by SET domains; and that the only invariant active site residue tyrosine 105 in vSET facilitates methyl transfer from cofactor to the substrate lysine by aligning intermolecular interactions in the lysine access channel of the enzyme. | ||
| - | + | Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase.,Qian C, Wang X, Manzur K, Sachchidanand, Farooq A, Zeng L, Wang R, Zhou MM J Mol Biol. 2006 May 26;359(1):86-96. Epub 2006 Mar 20. PMID:16603186<ref>PMID:16603186</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2g46" style="background-color:#fffaf0;"></div> |
| - | [[Category: Qian, C M | + | |
| - | [[Category: Zheng, L | + | ==See Also== |
| - | [[Category: Zhou, M M | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chlorella pbcv-1 virus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Qian, C M]] | ||
| + | [[Category: Zheng, L]] | ||
| + | [[Category: Zhou, M M]] | ||
[[Category: Hsitone methyltransferase]] | [[Category: Hsitone methyltransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Vset structure]] | [[Category: Vset structure]] | ||
Current revision
structure of vSET in complex with meK27 H3 Pept. and cofactor product SAH
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