4b0a: Difference between revisions
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<StructureSection load='4b0a' size='340' side='right'caption='[[4b0a]], [[Resolution|resolution]] 1.97Å' scene=''> | <StructureSection load='4b0a' size='340' side='right'caption='[[4b0a]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b0a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4b0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B0A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ngm|1ngm]], [[1nh2|1nh2]], [[1rm1|1rm1]], [[1tba|1tba]], [[1tbp|1tbp]], [[1ytb|1ytb]], [[1ytf|1ytf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ngm|1ngm]], [[1nh2|1nh2]], [[1rm1|1rm1]], [[1tba|1tba]], [[1tbp|1tbp]], [[1ytb|1ytb]], [[1ytf|1ytf]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b0a OCA], [https://pdbe.org/4b0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b0a RCSB], [https://www.ebi.ac.uk/pdbsum/4b0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b0a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TAF1_YEAST TAF1_YEAST]] Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation 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.<ref>PMID:8980232</ref> <ref>PMID:10788514</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Baker's yeast]] | [[Category: Baker's yeast]] | ||
[[Category: Histone acetyltransferase]] | [[Category: Histone acetyltransferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Anandapadamanaban, M]] | [[Category: Anandapadamanaban, M]] | ||
[[Category: Andresen, C]] | [[Category: Andresen, C]] | ||
Revision as of 08:52, 25 August 2022
The high-resolution structure of yTBP-yTAF1 identifies conserved and competing interaction surfaces in transcriptional activationThe high-resolution structure of yTBP-yTAF1 identifies conserved and competing interaction surfaces in transcriptional activation
Structural highlights
Function[TAF1_YEAST] Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation 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.[1] [2] [3] [4] Publication Abstract from PubMedThe general transcription factor TFIID provides a regulatory platform for transcription initiation. Here we present the crystal structure (1.97 A) and NMR analysis of yeast TAF1 N-terminal domains TAND1 and TAND2 bound to yeast TBP, together with mutational data. We find that yeast TAF1-TAND1, which in itself acts as a transcriptional activator, binds TBP's concave DNA-binding surface by presenting similar anchor residues to TBP as does Mot1 but from a distinct structural scaffold. Furthermore, we show how TAF1-TAND2 uses an aromatic and acidic anchoring pattern to bind a conserved TBP surface groove traversing the basic helix region, and we find highly similar TBP-binding motifs also presented by the structurally distinct TFIIA, Mot1 and Brf1 proteins. Our identification of these anchoring patterns, which can be easily disrupted or enhanced, provides insight into the competitive multiprotein TBP interplay critical to transcriptional regulation. High-resolution structure of TBP with TAF1 reveals anchoring patterns in transcriptional regulation.,Anandapadamanaban M, Andresen C, Helander S, Ohyama Y, Siponen MI, Lundstrom P, Kokubo T, Ikura M, Moche M, Sunnerhagen M Nat Struct Mol Biol. 2013 Jul 14. doi: 10.1038/nsmb.2611. PMID:23851461[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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