Structural and biochemical characterization of a new Mg(2+) binding site near Tyr94 in the restriction endonuclease PvuII.

@article{Spyridaki2003StructuralAB,
  title={Structural and biochemical characterization of a new Mg(2+) binding site near Tyr94 in the restriction endonuclease PvuII.},
  author={Aspasia Spyridaki and Claudia Matzen and Thomas Lanio and Albert Jeltsch and A. Simoncsits and Alekos Athanasiadis and Eva Scheuring-Vanamee and Michael Kokkinidis and Alfred Pingoud},
  journal={Journal of molecular biology},
  year={2003},
  volume={331 2},
  pages={395-406}
}
We have determined the crystal structure of the PvuII endonuclease in the presence of Mg(2+). According to the structural data, divalent metal ion binding in the PvuII subunits is highly asymmetric. The PvuII-Mg(2+) complex has two distinct metal ion binding sites, one in each monomer. One site is formed by the catalytic residues Asp58 and Glu68, and has extensive similarities to a catalytically important site found in all structurally examined restriction endonucleases. The other binding site… CONTINUE READING