5m4s

From Proteopedia

(Difference between revisions)

Current revision

Transcription factor TFIIA as a single chain protein

Structural highlights

5m4s is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.38Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TF2AA_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.^[1] ^[2] 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.^[3]

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mitsiou DJ, Stunnenberg HG. TAC, a TBP-sans-TAFs complex containing the unprocessed TFIIAalphabeta precursor and the TFIIAgamma subunit. Mol Cell. 2000 Sep;6(3):527-37. PMID:11030333
↑ Zhou H, Spicuglia S, Hsieh JJ, Mitsiou DJ, Hoiby T, Veenstra GJ, Korsmeyer SJ, Stunnenberg HG. Uncleaved TFIIA is a substrate for taspase 1 and active in transcription. Mol Cell Biol. 2006 Apr;26(7):2728-35. PMID:16537915 doi:26/7/2728
↑ Mitsiou DJ, Stunnenberg HG. TAC, a TBP-sans-TAFs complex containing the unprocessed TFIIAalphabeta precursor and the TFIIAgamma subunit. Mol Cell. 2000 Sep;6(3):527-37. PMID:11030333
↑ 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. Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID. Elife. 2017 Nov 7;6. doi: 10.7554/eLife.30395. PMID:29111974 doi:http://dx.doi.org/10.7554/eLife.30395

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5m4s"

Categories: Homo sapiens | Large Structures | Gupta K | Kandiah E

@@ Line 1: / Line 1: @@
 ==Transcription factor TFIIA as a single chain protein==
-<StructureSection load='5m4s' size='340' side='right' caption='[[5m4s]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+<StructureSection load='5m4s' size='340' side='right'caption='[[5m4s]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[5m4s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5M4S FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</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=5m4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m4s OCA], [https://pdbe.org/5m4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m4s RCSB], [https://www.ebi.ac.uk/pdbsum/5m4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m4s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[https://www.uniprot.org/uniprot/TF2AA_HUMAN TF2AA_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> <ref>PMID:16537915</ref> [https://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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5m4s" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Gupta, K]]
+[[Category: Homo sapiens]]
-[[Category: Kandiah, E]]
+[[Category: Large Structures]]
-[[Category: Single chain]]
+[[Category: Gupta K]]
-[[Category: Tfiia]]
+[[Category: Kandiah E]]
-[[Category: Tfiid]]
-[[Category: Transcription]]

5m4s

From Proteopedia

Current revision

Transcription factor TFIIA as a single chain protein

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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