Structure of the recA protein–ADP complex

@article{Story1992StructureOT,
  title={Structure of the recA protein–ADP complex},
  author={Randall M. Story and Thomas A Steitz},
  journal={Nature},
  year={1992},
  volume={355},
  pages={374-376}
}
THE recA protein catalyses the ATP-driven homologous pairing and strand exchange of DNA molecules1–3. It is an allosteric enzyme: the ATPase activity is DNA-dependent4,5, and ATP-bound recA protein has a high affinity for DNA, whereas the ADP-bound form has a low affinity6. In the absence of ATP hydrolysis, recA protein can still promote homologous pairing, apparently through the formation of a triple-stranded intermediate1,7–9. The exact role of ATP hydrolysis is not clear, but it presumably… CONTINUE READING
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