Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21.

@article{Kakuta2005CrystalSO,
  title={Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21.},
  author={Yoshimitsu Kakuta and Ikuko Ishimatsu and Tomoyuki Numata and Kazumi Kimura and Min Yao and Isao Tanaka and Makoto Kimura},
  journal={Biochemistry},
  year={2005},
  volume={44 36},
  pages={12086-93}
}
Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the removal of 5' leader sequences from tRNA precursors (pre-tRNA). The human protein Rpp21 is essential for human RNase P activity in tRNA processing in vitro. The crystal structure of Ph1601p from the hyperthermophilic archaeon Pyrococcus horikoshii OT3, the archaeal homologue of Rpp21, was determined using the multiple anomalous dispersion (MAD) method with the aid of anomalous scattering in zinc and selenium at 1.6 A… CONTINUE READING

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