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-Structure paper
タイトル | Structural basis of TFIIH activation for nucleotide excision repair. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 2885, Year 2019 |
掲載日 | 2019年6月28日 |
著者 | Goran Kokic / Aleksandar Chernev / Dimitry Tegunov / Christian Dienemann / Henning Urlaub / Patrick Cramer / |
PubMed 要旨 | Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large ...Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large multisubunit transcription factor IIH (TFIIH). Here we report the cryo-EM structure of an NER intermediate containing TFIIH and the NER factor XPA. Compared to its transcription conformation, the TFIIH structure is rearranged such that its ATPase subunits XPB and XPD bind double- and single-stranded DNA, consistent with their translocase and helicase activities, respectively. XPA releases the inhibitory kinase module of TFIIH, displaces a 'plug' element from the DNA-binding pore in XPD, and together with the NER factor XPG stimulates XPD activity. Our results explain how TFIIH is switched from a transcription to a repair factor, and provide the basis for a mechanistic analysis of the NER pathway. |
リンク | Nat Commun / PubMed:31253769 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.5 Å |
構造データ | |
化合物 | ChemComp-SF4: ChemComp-ZN: |
由来 |
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キーワード | TRANSLOCASE / Complex / Helicase / DNA repair |