8b8t | pdb_00008b8t

Open conformation of the complex of DNA ligase I on PCNA and DNA in the presence of ATP

spinqualitylabelsall models 8b8t, resolution 4.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8b8t is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DNLI1_HUMAN DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Publication Abstract from PubMed During lagging strand synthesis, DNA Ligase 1 (Lig1) cooperates with the sliding clamp PCNA to seal the nicks between Okazaki fragments generated by Pol delta 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(N-term)) and DNA binding domain (PIP(DBD)). Once Lig1 and PCNA assemble as two-stack rings encircling DNA, PIP(N-term) is released from PCNA and only PIP(DBD) 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. Mechanism of human Lig1 regulation by PCNA in Okazaki fragment sealing.,Blair K, Tehseen M, Raducanu VS, Shahid T, Lancey C, Rashid F, Creuhet R, Hamdan SM, De Biasio A Nat Commun. 2022 Dec 20;13(1):7833. doi: 10.1038/s41467-022-35475-z. PMID:36539424 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA