2c5z

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[[Image:2c5z.png|left|200px]]
 
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{{STRUCTURE_2c5z| PDB=2c5z | SCENE= }}
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==Structure and CTD binding of the Set2 SRI domain==
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<StructureSection load='2c5z' size='340' side='right'caption='[[2c5z]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2c5z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C5Z 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">Solution NMR</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=2c5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c5z OCA], [https://pdbe.org/2c5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c5z RCSB], [https://www.ebi.ac.uk/pdbsum/2c5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c5z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SET2_YEAST SET2_YEAST] Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. The methyltransferase activity requires the recruitment to the RNA polymerase II, which is CTK1 dependent.<ref>PMID:11839797</ref> <ref>PMID:12629047</ref> <ref>PMID:12736296</ref> <ref>PMID:12773564</ref> <ref>PMID:12917322</ref> <ref>PMID:15798214</ref> <ref>PMID:16227595</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/c5/2c5z_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=2c5z 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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During mRNA elongation, the SRI domain of the histone H3 methyltransferase Set2 binds to the phosphorylated carboxyl-terminal domain (CTD) of RNA polymerase II. The solution structure of the yeast Set2 SRI domain reveals a novel CTD-binding fold consisting of a left-handed three-helix bundle. NMR titration shows that the SRI domain binds an Ser2/Ser5-phosphorylated CTD peptide comprising two heptapeptide repeats and three flanking NH2-terminal residues, whereas a single CTD repeat is insufficient for binding. Residues that show strong chemical shift perturbations upon CTD binding cluster in two regions. Both CTD tyrosine side chains contact the SRI domain. One of the tyrosines binds in the region with the strongest chemical shift perturbations, formed by the two NH2-terminal helices. Unexpectedly, the SRI domain fold resembles the structure of an RNA polymerase-interacting domain in bacterial sigma factors (domain sigma2 in sigma70).
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===STRUCTURE AND CTD BINDING OF THE SET2 SRI DOMAIN===
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Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI domain that couples histone H3 Lys36 methylation to transcription.,Vojnic E, Simon B, Strahl BD, Sattler M, Cramer P J Biol Chem. 2006 Jan 6;281(1):13-5. Epub 2005 Nov 14. PMID:16286474<ref>PMID:16286474</ref>
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{{ABSTRACT_PUBMED_16286474}}
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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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==About this Structure==
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<div class="pdbe-citations 2c5z" style="background-color:#fffaf0;"></div>
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[[2c5z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5Z OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016286474</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Cramer, P.]]
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[[Category: Cramer P]]
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[[Category: Sattler, M.]]
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[[Category: Sattler M]]
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[[Category: Simon, B.]]
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[[Category: Simon B]]
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[[Category: Strahl, B D.]]
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[[Category: Strahl BD]]
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[[Category: Vojnic, E.]]
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[[Category: Vojnic E]]
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[[Category: Ctd]]
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[[Category: Rna polymerase ii]]
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[[Category: Set2 histone methyltransferase]]
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[[Category: Sri domain]]
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[[Category: Transcription]]
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Current revision

Structure and CTD binding of the Set2 SRI domain

PDB ID 2c5z

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