ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.

@article{Petrova2012ATPdependentDL,
  title={ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.},
  author={Tatiana E. Petrova and Ekaterina Yu Bezsudnova and Konstantin M. Boyko and Andrey V Mardanov and Konstantin M Polyakov and Vladimir V. Volkov and Michael B. Kozin and Nikolai V. Ravin and Ivan G Shabalin and Konstantin G. Skryabin and Tatiana N. Stekhanova and Michael V Kovalchuk and Vladimir O. Popov},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2012},
  volume={68 Pt 12},
  pages={1440-7}
}
DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been… CONTINUE READING