7K01
Structure of TFIIH in TFIIH/Rad4-Rad23-Rad33 DNA opening complex
Summary for 7K01
Entry DOI | 10.2210/pdb7k01/pdb |
Related | 7K04 7M2U |
EMDB information | 22576 22587 |
Descriptor | General transcription and DNA repair factor IIH subunit TFB1, General transcription and DNA repair factor IIH subunit TFB4, DNA repair helicase RAD25, ... (9 entities in total) |
Functional Keywords | tfiih, rad4, rad4/23, xpc, ner, nucleotide excision repair, gg-ner, nuclear protein, nuclear protein-transferase complex, nuclear protein/transferase |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 7 |
Total formula weight | 415754.98 |
Authors | |
Primary citation | van Eeuwen, T.,Shim, Y.,Kim, H.J.,Zhao, T.,Basu, S.,Garcia, B.A.,Kaplan, C.D.,Min, J.H.,Murakami, K. Cryo-EM structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair. Nat Commun, 12:3338-3338, 2021 Cited by PubMed Abstract: The versatile nucleotide excision repair (NER) pathway initiates as the XPC-RAD23B-CETN2 complex first recognizes DNA lesions from the genomic DNA and recruits the general transcription factor complex, TFIIH, for subsequent lesion verification. Here, we present a cryo-EM structure of an NER initiation complex containing Rad4-Rad23-Rad33 (yeast homologue of XPC-RAD23B-CETN2) and 7-subunit coreTFIIH assembled on a carcinogen-DNA adduct lesion at 3.9-9.2 Å resolution. A ~30-bp DNA duplex could be mapped as it straddles between Rad4 and the Ssl2 (XPB) subunit of TFIIH on the 3' and 5' side of the lesion, respectively. The simultaneous binding with Rad4 and TFIIH was permitted by an unwinding of DNA at the lesion. Translocation coupled with torque generation by Ssl2 and Rad4 would extend the DNA unwinding at the lesion and deliver the damaged strand to Rad3 (XPD) in an open form suitable for subsequent lesion scanning and verification. PubMed: 34099686DOI: 10.1038/s41467-021-23684-x PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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