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4wfq

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Revision as of 17:06, 22 March 2017

Crystal structure of TFIIH subunit

Structural highlights

4wfq is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SSL1_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. SSL1 is essential for translation initiation.^[1] ^[2]

Publication Abstract from PubMed

The Ssl1/p44 subunit is a core component of the yeast/mammalian general transcription factor TFIIH, which is involved in transcription and DNA repair. Ssl1/p44 binds to and stimulates the Rad3/XPD helicase activity of TFIIH. To understand the helicase stimulatory mechanism of Ssl1/p44, we determined the crystal structure of the N-terminal regulatory domain of Ssl1 from Saccharomyces cerevisiae. Ssl1 forms a von Willebrand factor A fold in which a central six-stranded beta-sheet is sandwiched between three alpha helices on both sides. Structural and biochemical analyses of Ssl1/p44 revealed that the beta4-alpha5 loop, which is frequently found at the interface between von Willebrand factor A family proteins and cellular counterparts, is critical for the stimulation of Rad3/XPD. Yeast genetics analyses showed that double mutation of Leu-239 and Ser-240 in the beta4-alpha5 loop of Ssl1 leads to lethality of a yeast strain, demonstrating the importance of the Rad3-Ssl1 interactions to cell viability. Here, we provide a structural model for the Rad3/XPD-Ssl1/p44 complex and insights into how the binding of Ssl1/p44 contributes to the helicase activity of Rad3/XPD and cell viability.

Crystal structure of the Rad3/XPD regulatory domain of Ssl1/p44.,Kim JS, Saint-Andre C, Lim HS, Hwang CS, Egly JM, Cho Y J Biol Chem. 2015 Mar 27;290(13):8321-30. doi: 10.1074/jbc.M115.636514. Epub 2015, Feb 13. PMID:25681444^[3]

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

References

↑ 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
↑ Kim JS, Saint-Andre C, Lim HS, Hwang CS, Egly JM, Cho Y. Crystal structure of the Rad3/XPD regulatory domain of Ssl1/p44. J Biol Chem. 2015 Mar 27;290(13):8321-30. doi: 10.1074/jbc.M115.636514. Epub 2015, Feb 13. PMID:25681444 doi:http://dx.doi.org/10.1074/jbc.M115.636514

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wfq"

Categories: Cho, Y | Kim, J S | Lim, H S | Helicase activator | Transcription

@@ Line 1: / Line 1: @@
 ==Crystal structure of TFIIH subunit==
 <StructureSection load='4wfq' size='340' side='right' caption='[[4wfq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4wfq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WFQ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4wfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wfq RCSB], [http://www.ebi.ac.uk/pdbsum/4wfq PDBsum]</span></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=4wfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfq OCA], [http://pdbe.org/4wfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wfq RCSB], [http://www.ebi.ac.uk/pdbsum/4wfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wfq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4wfq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4wfq

From Proteopedia

Revision as of 17:06, 22 March 2017

Crystal structure of TFIIH subunit

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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