6RO4
Structure of the core TFIIH-XPA-DNA complex
Summary for 6RO4
| Entry DOI | 10.2210/pdb6ro4/pdb |
| EMDB information | 4970 |
| Descriptor | DNA1, IRON/SULFUR CLUSTER, ZINC ION, ... (11 entities in total) |
| Functional Keywords | complex, helicase, translocase, dna repair |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 9 |
| Total formula weight | 377907.84 |
| Authors | Kokic, G.,Chernev, A.,Tegunov, D.,Dienemann, C.,Urlaub, H.,Cramer, P. (deposition date: 2019-05-10, release date: 2019-07-03, Last modification date: 2024-05-22) |
| Primary citation | Kokic, G.,Chernev, A.,Tegunov, D.,Dienemann, C.,Urlaub, H.,Cramer, P. Structural basis of TFIIH activation for nucleotide excision repair. Nat Commun, 10:2885-2885, 2019 Cited by PubMed Abstract: 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. PubMed: 31253769DOI: 10.1038/s41467-019-10745-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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