4WFQ

Crystal structure of TFIIH subunit

Summary for 4WFQ

• Entry DOI: 10.2210/pdb4wfq/pdb
• Descriptor: Suppressor of stem-loop protein 1, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: helicase activator, transcription
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus : Q04673
• Total number of polymer chains: 1
• Total formula weight: 21597.94

Authors

Cho, Y.,Kim, J.S.,Lim, H.S. (deposition date: 2014-09-17, release date: 2015-02-18, Last modification date: 2024-03-20)

Primary citation

Kim, J.S.,Saint-Andre, C.,Lim, H.S.,Hwang, C.S.,Egly, J.M.,Cho, Y.
Crystal structure of the Rad3/XPD regulatory domain of Ssl1/p44
J.Biol.Chem., 290:8321-8330, 2015

PubMed Abstract: 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 β-sheet is sandwiched between three α helices on both sides. Structural and biochemical analyses of Ssl1/p44 revealed that the β4-α5 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 β4-α5 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.

PubMed: 25681444
DOI: 10.1074/jbc.M115.636514

Experimental method

X-RAY DIFFRACTION (2.4 Å)