Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.

@article{Yamada2001CrystalSO,
  title={Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.},
  author={Kazuhiro Yamada and Naoki Kunishima and Kouta Mayanagi and Takayuki Ohnishi 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={2001},
  volume={98 4},
  pages={
          1442-7
        }
}
We report here the crystal structure of the RuvB motor protein from Thermus thermophilus HB8, which drives branch migration of the Holliday junction during homologous recombination. RuvB has a crescent-like architecture consisting of three consecutive domains, the first two of which are involved in ATP binding and hydrolysis. DNA is likely to interact with a large basic cleft, which encompasses the ATP-binding pocket and domain boundaries, whereas the junction-recognition protein RuvA may bind… CONTINUE READING
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