Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates.

ABSTRACT: DNA ligases are the sine qua non of genome integrity and essential for DNA replication and repair in all organisms. DNA ligases join 3'-OH and 5'-PO₄ ends via a series of three nucleotidyl transfer steps. In step 1, ligase reacts with ATP or NAD⁺ to form a covalent ligase-(lysyl-Nζ)-AMP intermediate and release pyrophosphate (PP_i) or nicotinamide mononucleotide. In step 2, AMP is transferred from ligase-adenylate to the 5'-PO₄ DNA end to form a DNA-adenylate intermediate (AppDNA). In step 3, ligase catalyzes attack by a DNA 3'-OH on the DNA-adenylate to seal the two ends via a phosphodiester bond and release AMP. Eukaryal, archaeal, and many bacterial and viral DNA ligases are ATP-dependent. The catalytic core of ATP-dependent DNA ligases

SUBMITTER: Unciuleac MC 

PROVIDER: S-EPMC6442053 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature