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7QNZ

human Lig1-DNA-PCNA complex reconstituted in absence of ATP

Summary for 7QNZ
Entry DOI10.2210/pdb7qnz/pdb
EMDB information14078
DescriptorDNA ligase 1, Proliferating cell nuclear antigen, Oligo19ddC, ... (6 entities in total)
Functional Keywordsdna, replication, complex, ligase, pcna, ligation, okazaki fragment maturation
Biological sourceHomo sapiens (human)
More
Total number of polymer chains7
Total formula weight209113.19
Authors
Blair, K.,Tehseen, M.,Raducanu, V.S.,Shahid, T.,Lancey, C.,Cruehet, R.,Hamdan, S.,De Biasio, A. (deposition date: 2021-12-23, release date: 2023-01-11, Last modification date: 2024-07-17)
Primary citationBlair, K.,Tehseen, M.,Raducanu, V.S.,Shahid, T.,Lancey, C.,Rashid, F.,Creuhet, R.,Hamdan, S.M.,De Biasio, A.
Mechanism of human Lig1 regulation by PCNA in Okazaki fragment sealing.
Nat Commun, 13:7833-7833, 2022
Cited by
PubMed Abstract: During lagging strand synthesis, DNA Ligase 1 (Lig1) cooperates with the sliding clamp PCNA to seal the nicks between Okazaki fragments generated by Pol δ and Flap endonuclease 1 (FEN1). We present several cryo-EM structures combined with functional assays, showing that human Lig1 recruits PCNA to nicked DNA using two PCNA-interacting motifs (PIPs) located at its disordered N-terminus (PIP) and DNA binding domain (PIP). Once Lig1 and PCNA assemble as two-stack rings encircling DNA, PIP is released from PCNA and only PIP is required for ligation to facilitate the substrate handoff from FEN1. Consistently, we observed that PCNA forms a defined complex with FEN1 and nicked DNA, and it recruits Lig1 to an unoccupied monomer creating a toolbelt that drives the transfer of DNA to Lig1. Collectively, our results provide a structural model on how PCNA regulates FEN1 and Lig1 during Okazaki fragments maturation.
PubMed: 36539424
DOI: 10.1038/s41467-022-35475-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.58 Å)
Structure validation

227344

數據於2024-11-13公開中

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