View source for 4atg


==TAF6 C-terminal domain from Antonospora locustae==
<StructureSection load='4atg' size='340' side='right'caption='[[4atg]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4atg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Antonospora_locustae Antonospora locustae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ATG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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=4atg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atg OCA], [https://pdbe.org/4atg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atg RCSB], [https://www.ebi.ac.uk/pdbsum/4atg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I6L8L5_ANTLO I6L8L5_ANTLO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The general transcription factor TFIID recognizes specifically the core promoter of genes transcribed by eukaryotic RNA Polymerase II, nucleating the assembly of the pre-initiation complex at the transcription start site. Yet, the understanding in molecular terms of TFIID assembly and function remains poorly understood. Histone fold motifs have been shown to be extremely important for the heterodimerization of many TFIID subunits. However, these subunits display several evolutionary conserved non-canonical features compared to histones, including additional regions whose role is unknown. Here we show that the conserved additional C-terminal region of TFIID subunit TAF6 can be divided into two domains: a small middle domain (TAF6M) and a large C-terminal domain (TAF6C). Our crystal structure of the TAF6C domain from Antonospora locustae at 1.9 A resolution reveals the presence of five conserved HEAT-repeats. Based on these data, we designed several mutants that were introduced into full-length human TAF6. Surprisingly, the mutants affect the interaction between TAF6 and TAF9, suggesting that the formation of the complex between these two TFIID subunits do not only depend on their histone fold motifs. In addition, the same mutants affect even more strongly the interaction between TAF6 and TAF9 in the context of a TAF5/TAF6/TAF9 complex. Expression of these mutants in HeLa cells reveals that most of them are unstable, suggesting their poor incorporation within endogeneous TFIID. Taken together, our results suggest that the conserved additional domains in histone fold-containing subunits of TFIID and of co-activator SAGA are important for the assembly of these complexes.

TFIID TAF6/TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5.,Scheer E, Delbac F, Tora L, Moras D, Romier C J Biol Chem. 2012 Jun 13. PMID:22696218<ref>PMID:22696218</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4atg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Antonospora locustae]]
[[Category: Large Structures]]
[[Category: Romier C]]