8REV
Structure of XPD stalled at a Y-fork DNA containing a interstrand crosslink
Summary for 8REV
| Entry DOI | 10.2210/pdb8rev/pdb |
| EMDB information | 19109 |
| Descriptor | ATP-dependent DNA helicase CHL1, General transcription and DNA repair factor IIH, DNA (47-MER), ... (6 entities in total) |
| Functional Keywords | damaged dna, helicase, xpd, ner, dna repair, interstrand crosslink, dna binding protein |
| Biological source | Thermochaetoides thermophila More |
| Total number of polymer chains | 4 |
| Total formula weight | 179502.09 |
| Authors | Kuper, J.,Hove, T.,Kisker, C. (deposition date: 2023-12-12, release date: 2024-05-29, Last modification date: 2024-10-30) |
| Primary citation | Kuper, J.,Hove, T.,Maidl, S.,Neitz, H.,Sauer, F.,Kempf, M.,Schroeder, T.,Greiter, E.,Hobartner, C.,Kisker, C. XPD stalled on cross-linked DNA provides insight into damage verification. Nat.Struct.Mol.Biol., 31:1580-1588, 2024 Cited by PubMed Abstract: The superfamily 2 helicase XPD is a central component of the general transcription factor II H (TFIIH), which is essential for transcription and nucleotide excision DNA repair (NER). Within these two processes, the helicase function of XPD is vital for NER but not for transcription initiation, where XPD acts only as a scaffold for other factors. Using cryo-EM, we deciphered one of the most enigmatic steps in XPD helicase action: the active separation of double-stranded DNA (dsDNA) and its stalling upon approaching a DNA interstrand cross-link, a highly toxic form of DNA damage. The structure shows how dsDNA is separated and reveals a highly unusual involvement of the Arch domain in active dsDNA separation. Combined with mutagenesis and biochemical analyses, we identified distinct functional regions important for helicase activity. Surprisingly, those areas also affect core TFIIH translocase activity, revealing a yet unencountered function of XPD within the TFIIH scaffold. In summary, our data provide a universal basis for NER bubble formation, XPD damage verification and XPG incision. PubMed: 38806694DOI: 10.1038/s41594-024-01323-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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