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==Crystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9cr==
==Crystal structure of Taf14 YEATS domain G82A mutant in complex with histone H3K9cr==
<StructureSection load='6min' size='340' side='right' caption='[[6min]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6min' size='340' side='right'caption='[[6min]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6min]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MIN FirstGlance]. <br>
<table><tr><td colspan='2'>[[6min]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MIN FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=KCR:N-6-CROTONYL-L-LYSINE'>KCR</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=6min FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6min OCA], [http://pdbe.org/6min PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6min RCSB], [http://www.ebi.ac.uk/pdbsum/6min PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6min ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=KCR:N-6-CROTONYL-L-LYSINE'>KCR</scene></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=6min FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6min OCA], [https://pdbe.org/6min PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6min RCSB], [https://www.ebi.ac.uk/pdbsum/6min PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6min ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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> 
[https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN]  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6min" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6min" style="background-color:#fffaf0;"></div>
==See Also==
*[[Histone 3D structures|Histone 3D structures]]
*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Andrews, F H]]
[[Category: Homo sapiens]]
[[Category: Klein, B J]]
[[Category: Large Structures]]
[[Category: Kutateladze, T G]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Epigenetic]]
[[Category: Andrews FH]]
[[Category: Histone reader]]
[[Category: Klein BJ]]
[[Category: Transcription]]
[[Category: Kutateladze TG]]

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