1n3j

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[[Image:1n3j.jpg|left|200px]]
 
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{{Structure
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==Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1==
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|PDB= 1n3j |SIZE=350|CAPTION= <scene name='initialview01'>1n3j</scene>
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<StructureSection load='1n3j' size='340' side='right'caption='[[1n3j]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1n3j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_bursaria_Chlorella_virus_1 Paramecium bursaria Chlorella virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N3J FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= A612L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10506 Paramecium bursaria Chlorella virus 1])
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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=1n3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3j OCA], [https://pdbe.org/1n3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n3j RCSB], [https://www.ebi.ac.uk/pdbsum/1n3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n3j ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O41094_PBCV1 O41094_PBCV1]
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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/n3/1n3j_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=1n3j 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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Site-specific lysine methylation of histones by SET domains is a hallmark for epigenetic control of gene transcription in eukaryotic organisms. Here we report that a SET domain protein from Paramecium bursaria chlorella virus can specifically di-methylate Lys27 in histone H3, a modification implicated in gene silencing. The solution structure of the viral SET domain reveals a butterfly-shaped head-to-head symmetric dimer different from other known protein methyltransferases. Each subunit consists of a Greek-key antiparallel beta-barrel and a three-stranded open-faced sandwich that mediates the dimer interface. Cofactor S-adenosyl-L-methionine (SAM) binds at the opening of the beta-barrel, and amino acids C-terminal to Lys27 in H3 and in the flexible C-terminal tail of the enzyme confer the specificity of this viral histone methyltransferase.
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'''Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1'''
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A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3.,Manzur KL, Farooq A, Zeng L, Plotnikova O, Koch AW, Sachchidanand, Zhou MM Nat Struct Biol. 2003 Mar;10(3):187-96. PMID:12567185<ref>PMID:12567185</ref>
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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 1n3j" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Site-specific lysine methylation of histones by SET domains is a hallmark for epigenetic control of gene transcription in eukaryotic organisms. Here we report that a SET domain protein from Paramecium bursaria chlorella virus can specifically di-methylate Lys27 in histone H3, a modification implicated in gene silencing. The solution structure of the viral SET domain reveals a butterfly-shaped head-to-head symmetric dimer different from other known protein methyltransferases. Each subunit consists of a Greek-key antiparallel beta-barrel and a three-stranded open-faced sandwich that mediates the dimer interface. Cofactor S-adenosyl-L-methionine (SAM) binds at the opening of the beta-barrel, and amino acids C-terminal to Lys27 in H3 and in the flexible C-terminal tail of the enzyme confer the specificity of this viral histone methyltransferase.
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1N3J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3J OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3., Manzur KL, Farooq A, Zeng L, Plotnikova O, Koch AW, Sachchidanand, Zhou MM, Nat Struct Biol. 2003 Mar;10(3):187-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12567185 12567185]
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[[Category: Paramecium bursaria Chlorella virus 1]]
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[[Category: Paramecium bursaria chlorella virus 1]]
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[[Category: Farooq A]]
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[[Category: Single protein]]
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[[Category: Koch AW]]
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[[Category: Farooq, A.]]
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[[Category: Manzur KL]]
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[[Category: Koch, A W.]]
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[[Category: Plotnikova O]]
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[[Category: Manzur, K L.]]
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[[Category: Plotnikova, O.]]
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[[Category: Sachchidanand]]
[[Category: Sachchidanand]]
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[[Category: Zeng, L.]]
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[[Category: Zeng L]]
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[[Category: Zhou, M M.]]
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[[Category: Zhou M-M]]
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[[Category: beta barrel]]
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[[Category: homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:51:44 2008''
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Current revision

Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1

PDB ID 1n3j

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