Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.

@article{Ariyoshi2000CrystalSO,
  title={Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.},
  author={Mariko Ariyoshi and Tatsuya Nishino and Hiroshi Iwasaki and Hideo Shinagawa and Kosuke Morikawa},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 15},
  pages={8257-62}
}
In the major pathway of homologous DNA recombination in prokaryotic cells, the Holliday junction intermediate is processed through its association with RuvA, RuvB, and RuvC proteins. Specific binding of the RuvA tetramer to the Holliday junction is required for the RuvB motor protein to be loaded onto the junction DNA, and the RuvAB complex drives the ATP-dependent branch migration. We solved the crystal structure of the Holliday junction bound to a single Escherichia coli RuvA tetramer at 3.1… CONTINUE READING