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5m4s

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'''Unreleased structure'''
 
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The entry 5m4s is ON HOLD until Paper Publication
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==Transcription factor TFIIA as a single chain protein==
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<StructureSection load='5m4s' size='340' side='right' caption='[[5m4s]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5m4s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M4S FirstGlance]. <br>
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</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=5m4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m4s OCA], [http://pdbe.org/5m4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m4s RCSB], [http://www.ebi.ac.uk/pdbsum/5m4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m4s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/T2AG_HUMAN T2AG_HUMAN]] TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.<ref>PMID:11030333</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain-containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function.
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Authors:
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Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.,Gupta K, Watson AA, Baptista T, Scheer E, Chambers AL, Koehler C, Zou J, Obong-Ebong I, Kandiah E, Temblador A, Round A, Forest E, Man P, Bieniossek C, Laue ED, Lemke EA, Rappsilber J, Robinson CV, Devys D, Tora L, Berger I Elife. 2017 Nov 7;6. doi: 10.7554/eLife.30395. PMID:29111974<ref>PMID:29111974</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5m4s" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gupta, K]]
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[[Category: Kandiah, E]]
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[[Category: Single chain]]
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[[Category: Tfiia]]
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[[Category: Tfiid]]
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[[Category: Transcription]]

Revision as of 06:06, 29 November 2017

Transcription factor TFIIA as a single chain protein

5m4s, resolution 2.38Å

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