Structural Biology of Rad50 ATPase ATP-Driven Conformational Control in DNA Double-Strand Break Repair and the ABC-ATPase Superfamily

@article{Hopfner2000StructuralBO,
  title={Structural Biology of Rad50 ATPase ATP-Driven Conformational Control in DNA Double-Strand Break Repair and the ABC-ATPase Superfamily},
  author={Karl-Peter Hopfner and Annette Karcher and David Sj Shin and Lisa Craig and L.Matthew Arthur and James P. Carney and John A. Tainer},
  journal={Cell},
  year={2000},
  volume={101},
  pages={789-800}
}
To clarify the key role of Rad50 in DNA double-strand break repair (DSBR), we biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd displays ATPase activity plus ATP-controlled dimerization and DNA binding activities. Rad50cd crystal structures identify probable protein and DNA interfaces and reveal an ABC-ATPase fold, linking Rad50 molecular mechanisms to ABC transporters, including P glycoprotein and cystic… CONTINUE READING
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