4wfq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4wfq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4WFQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4wfq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4WFQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4wfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfq OCA], [https://pdbe.org/4wfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wfq RCSB], [https://www.ebi.ac.uk/pdbsum/4wfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wfq 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=4wfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfq OCA], [https://pdbe.org/4wfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wfq RCSB], [https://www.ebi.ac.uk/pdbsum/4wfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wfq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SSL1_YEAST 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.<ref>PMID:7961739</ref> <ref>PMID:8631896</ref>  
[https://www.uniprot.org/uniprot/SSL1_YEAST 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.<ref>PMID:7961739</ref> <ref>PMID:8631896</ref>  
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25681444</ref>
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 ==
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