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8BOT

Cryo-EM structure of NHEJ supercomplex(trimer)

This is a non-PDB format compatible entry.
Summary for 8BOT
Entry DOI10.2210/pdb8bot/pdb
EMDB information16145
DescriptorDNA repair protein XRCC4, DNA (24-MER), DNA ligase 4, ... (10 entities in total)
Functional Keywordsnhej, dna-pk, dna-pkcs, ku70, ku80, xlf, dna repair, dna binding protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains25
Total formula weight2411092.49
Authors
Hardwick, S.W.,Chaplin, A.K. (deposition date: 2022-11-15, release date: 2023-06-28, Last modification date: 2023-08-16)
Primary citationHardwick, S.W.,Stavridi, A.K.,Chirgadze, D.Y.,De Oliveira, T.M.,Charbonnier, J.B.,Ropars, V.,Meek, K.,Blundell, T.L.,Chaplin, A.K.
Cryo-EM structure of a DNA-PK trimer: higher order oligomerisation in NHEJ.
Structure, 31:895-, 2023
Cited by
PubMed Abstract: The ability of humans to maintain the integrity of the genome is imperative for cellular survival. DNA double-strand breaks (DSBs) are considered the most critical type of DNA lesion, which can ultimately lead to diseases including cancer. Non-homologous end joining (NHEJ) is one of two core mechanisms utilized to repair DSBs. DNA-PK is a key component in this process and has recently been shown to form alternate long-range synaptic dimers. This has led to the proposal that these complexes can be formed before transitioning to a short-range synaptic complex. Here we present cryo-EM data representing an NHEJ supercomplex consisting of a trimer of DNA-PK in complex with XLF, XRCC4, and DNA Ligase IV. This trimer represents a complex of both long-range synaptic dimers. We discuss the potential role of the trimeric structure, and possible higher order oligomers, as structural intermediates in the NHEJ mechanism, or as functional DNA repair centers.
PubMed: 37311458
DOI: 10.1016/j.str.2023.05.013
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.76 Å)
Structure validation

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