8EBS
Initial DNA-lesion (Cy5) binding by XPC and TFIIH
Summary for 8EBS
| Entry DOI | 10.2210/pdb8ebs/pdb |
| Related | 8EBS 8EBT 8EBU 8EBV 8EBW 8EBX 8EBY |
| EMDB information | 27996 27997 27998 27999 28000 28001 28002 |
| Descriptor | TFIIH basal transcription factor complex helicase XPB subunit, Centrin-2, DNA (Cy5), ... (15 entities in total) |
| Functional Keywords | protein-dna complex, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 12 |
| Total formula weight | 585993.63 |
| Authors | |
| Primary citation | Kim, J.,Li, C.L.,Chen, X.,Cui, Y.,Golebiowski, F.M.,Wang, H.,Hanaoka, F.,Sugasawa, K.,Yang, W. Lesion recognition by XPC, TFIIH and XPA in DNA excision repair. Nature, 617:170-175, 2023 Cited by PubMed Abstract: Nucleotide excision repair removes DNA lesions caused by ultraviolet light, cisplatin-like compounds and bulky adducts. After initial recognition by XPC in global genome repair or a stalled RNA polymerase in transcription-coupled repair, damaged DNA is transferred to the seven-subunit TFIIH core complex (Core7) for verification and dual incisions by the XPF and XPG nucleases. Structures capturing lesion recognition by the yeast XPC homologue Rad4 and TFIIH in transcription initiation or DNA repair have been separately reported. How two different lesion recognition pathways converge and how the XPB and XPD helicases of Core7 move the DNA lesion for verification are unclear. Here we report on structures revealing DNA lesion recognition by human XPC and DNA lesion hand-off from XPC to Core7 and XPA. XPA, which binds between XPB and XPD, kinks the DNA duplex and shifts XPC and the DNA lesion by nearly a helical turn relative to Core7. The DNA lesion is thus positioned outside of Core7, as would occur with RNA polymerase. XPB and XPD, which track the lesion-containing strand but translocate DNA in opposite directions, push and pull the lesion-containing strand into XPD for verification. PubMed: 37076618DOI: 10.1038/s41586-023-05959-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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