9ZP0 image
Deposition Date 2025-12-16
Release Date 2026-09-16
Last Version Date 2026-10-21
Entry Detail
PDB ID:
9ZP0
Title:
CryoEM structure of DNA-PK bound to N0 nucleosome
Biological Source:
Source Organism(s):
Xenopus laevis (Taxon ID: 8355)
Homo sapiens (Taxon ID: 9606)
Method Details:
Experimental Method:
Resolution:
4.11 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:Histone H3
Gene (Uniprot):LOC121398065
Chain IDs:B (auth: A), F (auth: E)
Chain Length:99
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H4
Chain IDs:C (auth: B), G (auth: F)
Chain Length:87
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H2A
Gene (Uniprot):LOC494591
Chain IDs:D (auth: C), H (auth: G)
Chain Length:111
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H2B
Gene (Uniprot):LOC108704302
Chain IDs:E (auth: D), I (auth: H)
Chain Length:96
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (147-MER)
Chain IDs:A (auth: I)
Chain Length:147
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (147-MER)
Chain IDs:J
Chain Length:147
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:X-ray repair cross-complement
Gene (Uniprot):XRCC6
Chain IDs:M (auth: K)
Chain Length:609
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:DNA repair protein Ku80
Gene (Uniprot):XRCC5
Chain IDs:N (auth: L)
Chain Length:732
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:DNA-dependent protein kinase
Gene (Uniprot):PRKDC
Chain IDs:K (auth: M)
Chain Length:4128
Number of Molecules:1
Biological Source:Homo sapiens
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Unknown peptide
Chain IDs:L (auth: N)
Chain Length:20
Number of Molecules:1
Biological Source:Homo sapiens
Ligand Molecules
Primary Citation
DNA-PK driven nucleosome unwrapping enables NHEJ in chromatin.
Nat Commun 17 ? ? (2026)
PMID: 42838959 DOI: 10.1038/s41467-026-77534-9

Abstact

DNA double-strand breaks, one of the most cytotoxic forms of DNA damage, are primarily repaired by non-homologous end joining (NHEJ) in human cells. NHEJ is initiated by the Ku70/80 heterodimer (Ku) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs), followed by factors that bridge and ligate DNA ends. Ku and DNA-PKcs require ~28 base pairs of free duplex DNA, which is often unavailable in chromatin with nucleosomes acting as barriers. The role of DNA-PKcs remains unclear, as previous in vitro studies mainly used naked DNA. Here, in vitro ligation assays show that DNA-PKcs promotes NHEJ on nucleosomes with limited DNA accessibility. Cryo-EM structures of nucleosome-bound Ku and DNA-PKcs reveal that Ku encounters nucleosomal barriers and overcomes them with DNA-PKcs. Distinct structural states support a stepwise model of DNA-PK progressive translocating along nucleosomal DNA, highlighting DNA-PKcs function in chromatin-associated NHEJ in vivo.

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Primary Citation of related structures
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