5d7e: Difference between revisions

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-'''Unreleased structure'''
-The entry 5d7e is ON HOLD  until Paper Publication
+==Crystal structure of Taf14 YEATS domain in complex with H3K9ac==
+<StructureSection load='5d7e' size='340' side='right' caption='[[5d7e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5d7e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D7E FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d7e OCA], [http://pdbe.org/5d7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d7e RCSB], [http://www.ebi.ac.uk/pdbsum/5d7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d7e ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TAF14_YEAST TAF14_YEAST]] Functions as a component of the DNA-binding general transcription factor complex TFIID, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.<ref>PMID:9618449</ref> <ref>PMID:10788514</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref> <ref>PMID:12672490</ref> <ref>PMID:17157260</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. Our findings establish a highly conserved acetyllysine reader function for the YEATS domain protein family and highlight the significance of this interaction for Taf14.
-Authors: Andrews, F.H., Shanle, E.K., Strahl, B.D., Kutateladze, T.G.
+Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response.,Shanle EK, Andrews FH, Meriesh H, McDaniel SL, Dronamraju R, DiFiore JV, Jha D, Wozniak GG, Bridgers JB, Kerschner JL, Krajewski K, Martin GM, Morrison AJ, Kutateladze TG, Strahl BD Genes Dev. 2015 Sep 1;29(17):1795-800. doi: 10.1101/gad.269977.115. PMID:26341557<ref>PMID:26341557</ref>
-Description: Crystal structure of Taf14 YEATS domain in complex with H3K9ac
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Strahl, B.D]]
+<div class="pdbe-citations 5d7e" style="background-color:#fffaf0;"></div>
-[[Category: Kutateladze, T.G]]
+== References ==
-[[Category: Shanle, E.K]]
+<references/>
-[[Category: Andrews, F.H]]
+__TOC__
+</StructureSection>
+[[Category: Andrews, F H]]
+[[Category: Kutateladze, T G]]
+[[Category: Shanle, E K]]
+[[Category: Strahl, B D]]
+[[Category: Acetylation histone yeats reader]]
+[[Category: Nuclear protein]]