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==HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS==
==HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS==
<StructureSection load='1bh9' size='340' side='right' caption='[[1bh9]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1bh9' size='340' side='right'caption='[[1bh9]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bh9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BH9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bh9]] is a 2 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=1BH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BH9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PMB:PARA-MERCURY-BENZENESULFONIC+ACID'>PMB</scene></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]] 2.6&#8491;</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=1bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh9 OCA], [http://pdbe.org/1bh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh9 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMB:PARA-MERCURY-BENZENESULFONIC+ACID'>PMB</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=1bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh9 OCA], [https://pdbe.org/1bh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bh9 RCSB], [https://www.ebi.ac.uk/pdbsum/1bh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TAF13_HUMAN TAF13_HUMAN]] TFIID beta-specific TAFII. [[http://www.uniprot.org/uniprot/TAF11_HUMAN TAF11_HUMAN]] Core TAFII present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively).  
[https://www.uniprot.org/uniprot/TAF13_HUMAN TAF13_HUMAN] TFIID beta-specific TAFII.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1bh9 ConSurf].
</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=1bh9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28 and hTAF(II)18 were not predicted from their primary sequence, indicating that these TAF(II)s define a novel family of atypical histone fold sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also present in the N- and C-terminal regions of the SPT3 proteins, suggesting that the histone fold in SPT3 may be reconstituted by intramolecular rather than classical intermolecular interactions. The existence of additional histone-like pairs in both the TFIID and SAGA complexes shows that the histone fold is a more commonly used motif for mediating TAF-TAF interactions than previously believed.
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family.,Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D Cell. 1998 Jul 24;94(2):239-49. PMID:9695952<ref>PMID:9695952</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bh9" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transcription initiation factor|Transcription initiation factor]]
*[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Birck, C]]
[[Category: Large Structures]]
[[Category: Davidson, I]]
[[Category: Birck C]]
[[Category: Lavigne, A C]]
[[Category: Davidson I]]
[[Category: Mengus, G]]
[[Category: Lavigne A-C]]
[[Category: Moras, D]]
[[Category: Mengus G]]
[[Category: Poch, O]]
[[Category: Moras D]]
[[Category: Romier, C]]
[[Category: Poch O]]
[[Category: Ruff, M]]
[[Category: Romier C]]
[[Category: Histone fold]]
[[Category: Ruff M]]
[[Category: Htafii18]]
[[Category: Tata binding protein]]
[[Category: Transcription regulation complex]]

Latest revision as of 09:36, 7 February 2024

HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBSHTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS

Structural highlights

1bh9 is a 2 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 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TAF13_HUMAN TFIID beta-specific TAFII.

Evolutionary Conservation

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

See Also

1bh9, resolution 2.60Å

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