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[[Image:1ngm.gif|left|200px]]<br /><applet load="1ngm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ngm, resolution 2.95&Aring;" />
'''Crystal structure of a yeast Brf1-TBP-DNA ternary complex'''<br />


==Overview==
==Crystal structure of a yeast Brf1-TBP-DNA ternary complex==
Transcription factor IIIB (TFIIIB), consisting of the TATA-binding protein (TBP), TFIIB-related factor (Brf1) and Bdp1, is a central component in basal and regulated transcription by RNA polymerase III. TFIIIB recruits its polymerase to the promoter and subsequently has an essential role in the formation of the open initiation complex. The amino-terminal half of Brf1 shares a high degree of sequence similarity with the polymerase II general transcription factor TFIIB, but it is the carboxy-terminal half of Brf1 that contributes most of its binding affinity with TBP. The principal anchoring region is located between residues 435 and 545 of yeast Brf1, comprising its homology domain II. The same region also provides the primary interface for assembling Bdp1 into the TFIIIB complex. We report here a 2.95 A resolution crystal structure of the ternary complex containing Brf1 homology domain II, the conserved region of TBP and 19 base pairs of U6 promoter DNA. The structure reveals the core interface for assembly of TFIIIB and demonstrates how the loosely packed Brf1 domain achieves remarkable binding specificity with the convex and lateral surfaces of TBP.
<StructureSection load='1ngm' size='340' side='right'caption='[[1ngm]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ngm]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NGM 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]] 2.95&#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=1ngm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ngm OCA], [https://pdbe.org/1ngm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ngm RCSB], [https://www.ebi.ac.uk/pdbsum/1ngm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ngm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TBP_YEAST TBP_YEAST] General transcription factor that functions at the core 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 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.<ref>PMID:9618449</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ng/1ngm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ngm ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NGM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NGM OCA].
*[[TATA-binding protein 3D structures|TATA-binding protein 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of a transcription factor IIIB core interface ternary complex., Juo ZS, Kassavetis GA, Wang J, Geiduschek EP, Sigler PB, Nature. 2003 Apr 3;422(6931):534-9. Epub 2003 Mar 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12660736 12660736]
__TOC__
[[Category: Protein complex]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Geiduschek, E P.]]
[[Category: Geiduschek EP]]
[[Category: Juo, Z S.]]
[[Category: Juo ZS]]
[[Category: Kassavetis, G A.]]
[[Category: Kassavetis GA]]
[[Category: Sigler, P B.]]
[[Category: Sigler PB]]
[[Category: Wang, J.]]
[[Category: Wang J]]
[[Category: brf]]
[[Category: brf1]]
[[Category: protein-dna complex]]
[[Category: taf]]
[[Category: tbp]]
[[Category: tfiiib]]
[[Category: transcription]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:52 2008''

Latest revision as of 10:56, 14 February 2024

Crystal structure of a yeast Brf1-TBP-DNA ternary complexCrystal structure of a yeast Brf1-TBP-DNA ternary complex

Structural highlights

1ngm is a 16 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.95Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TBP_YEAST General transcription factor that functions at the core 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 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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Hampsey M. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol Mol Biol Rev. 1998 Jun;62(2):465-503. PMID:9618449
  2. ↑ Sanders SL, Garbett KA, Weil PA. Molecular characterization of Saccharomyces cerevisiae TFIID. Mol Cell Biol. 2002 Aug;22(16):6000-13. PMID:12138208
  3. ↑ Martinez E. Multi-protein complexes in eukaryotic gene transcription. Plant Mol Biol. 2002 Dec;50(6):925-47. PMID:12516863

1ngm, resolution 2.95Å

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