3dom: Difference between revisions

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<StructureSection load='3dom' size='340' side='right'caption='[[3dom]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3dom' size='340' side='right'caption='[[3dom]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dom]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DOM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dom]] is a 4 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=3DOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DOM FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dgp|3dgp]], [[1ydl|1ydl]], [[2jnj|2jnj]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TFB2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), TFB5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3dom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dom OCA], [https://pdbe.org/3dom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dom RCSB], [https://www.ebi.ac.uk/pdbsum/3dom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dom ProSAT]</span></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=3dom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dom OCA], [https://pdbe.org/3dom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dom RCSB], [https://www.ebi.ac.uk/pdbsum/3dom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dom ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TFB2_YEAST TFB2_YEAST]] Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro.<ref>PMID:9235928</ref> <ref>PMID:7961739</ref> <ref>PMID:8631896</ref>  [[https://www.uniprot.org/uniprot/TFB5_YEAST TFB5_YEAST]] Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro. TFB5 is required for stable recruitment of TFIIH to a promoter, but not for stability of TFIIH subunits.<ref>PMID:7961739</ref> <ref>PMID:8631896</ref>
[https://www.uniprot.org/uniprot/TFB5_YEAST TFB5_YEAST] Acts as component of the general transcription and DNA repair factor IIH (TFIIH) core, which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase activity, and is essential for polymerase II transcription in vitro. TFB5 is required for stable recruitment of TFIIH to a promoter, but not for stability of TFIIH subunits.<ref>PMID:7961739</ref> <ref>PMID:8631896</ref>  
== 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=3dom 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=3dom ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Patients with the rare neurodevelopmental repair syndrome known as group A trichothiodystrophy (TTD-A) carry mutations in the gene encoding the p8 subunit of the transcription and DNA repair factor TFIIH. Here we describe the crystal structure of a minimal complex between Tfb5, the yeast ortholog of p8, and the C-terminal domain of Tfb2, the yeast p52 subunit of TFIIH. The structure revealed that these two polypeptides adopt the same fold, forming a compact pseudosymmetric heterodimer via a beta-strand addition and coiled coils interactions between terminal alpha-helices. Furthermore, Tfb5 protects a hydrophobic surface in Tfb2 from solvent, providing a rationale for the influence of p8 in the stabilization of p52 and explaining why mutations that weaken p8-p52 interactions lead to a reduced intracellular TFIIH concentration and a defect in nucleotide-excision repair, a common feature of TTD cells.
Structural basis for group A trichothiodystrophy.,Kainov DE, Vitorino M, Cavarelli J, Poterszman A, Egly JM Nat Struct Mol Biol. 2008 Sep;15(9):980-4. PMID:19172752<ref>PMID:19172752</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3dom" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cavarelli, J]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Egly, J M]]
[[Category: Cavarelli J]]
[[Category: Kainov, D E]]
[[Category: Egly JM]]
[[Category: Poterszman, A]]
[[Category: Kainov DE]]
[[Category: Beta-alpha-beta split]]
[[Category: Poterszman A]]
[[Category: Beta-strand addition]]
[[Category: Dna damage]]
[[Category: Dna excision]]
[[Category: Dna repair]]
[[Category: Heterodimer]]
[[Category: Nucleus]]
[[Category: Protein-protein complex]]
[[Category: Transcription]]
[[Category: Transcription regulation]]

Latest revision as of 09:42, 21 February 2024

Crystal Structure of the complex between Tfb5 and the C-terminal domain of Tfb2

3dom, resolution 2.60Å

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