3dom

From Proteopedia

(Difference between revisions)

Revision as of 03:24, 25 December 2014

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

Structural highlights

3dom is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3dgp, 1ydl, 2jnj
Gene:	TFB2 (Saccharomyces cerevisiae), TFB5 (Saccharomyces cerevisiae)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] [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.^[4] ^[5]

Evolutionary Conservation

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

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^[6]

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

References

↑ Feaver WJ, Henry NL, Wang Z, Wu X, Svejstrup JQ, Bushnell DA, Friedberg EC, Kornberg RD. Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair factor IIH. Homology to human cyclin-dependent kinase activating kinase and IIH subunits. J Biol Chem. 1997 Aug 1;272(31):19319-27. PMID:9235928
↑ Svejstrup JQ, Feaver WJ, LaPointe J, Kornberg RD. RNA polymerase transcription factor IIH holoenzyme from yeast. J Biol Chem. 1994 Nov 11;269(45):28044-8. PMID:7961739
↑ Sung P, Guzder SN, Prakash L, Prakash S. Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair. J Biol Chem. 1996 May 3;271(18):10821-6. PMID:8631896
↑ Svejstrup JQ, Feaver WJ, LaPointe J, Kornberg RD. RNA polymerase transcription factor IIH holoenzyme from yeast. J Biol Chem. 1994 Nov 11;269(45):28044-8. PMID:7961739
↑ Sung P, Guzder SN, Prakash L, Prakash S. Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair. J Biol Chem. 1996 May 3;271(18):10821-6. PMID:8631896
↑ Kainov DE, Vitorino M, Cavarelli J, Poterszman A, Egly JM. Structural basis for group A trichothiodystrophy. Nat Struct Mol Biol. 2008 Sep;15(9):980-4. PMID:19172752

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dom"

@@ Line 7: / Line 7: @@
 <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=3dom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dom OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dom RCSB], [http://www.ebi.ac.uk/pdbsum/3dom PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://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>  [[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

3dom

From Proteopedia

Revision as of 03:24, 25 December 2014

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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