9ZP9 image
Deposition Date 2025-12-16
Release Date 2026-09-16
Last Version Date 2026-10-21
Entry Detail
PDB ID:
9ZP9
Title:
CryoEM structure of DNA-PK bound to N7 nucleosome, state 1
Biological Source:
Source Organism(s):
Xenopus laevis (Taxon ID: 8355)
Homo sapiens (Taxon ID: 9606)
Method Details:
Experimental Method:
Resolution:
3.88 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:Histone H3
Gene (Uniprot):LOC121398065
Chain IDs:A, E
Chain Length:112
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H4
Gene (Uniprot):His4
Chain IDs:B, F
Chain Length:87
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H2A
Chain IDs:C, G
Chain Length:111
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polypeptide(L)
Molecule:Histone H2B
Gene (Uniprot):LOC108704302
Chain IDs:D, H
Chain Length:96
Number of Molecules:2
Biological Source:Xenopus laevis
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (154-MER)
Chain IDs:I
Chain Length:154
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (154-MER)
Chain IDs:J
Chain Length:154
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:X-ray repair cross-complement
Gene (Uniprot):XRCC6
Chain IDs:K
Chain Length:609
Number of Molecules:1
Biological Source:Homo sapiens
Polymer Type:polypeptide(L)
Molecule:X-ray repair cross-complement
Gene (Uniprot):XRCC5
Chain IDs: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: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: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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