tRNase Z catalysis and conserved residues on the carboxy side of the His cluster.

@article{Karkashon2007tRNaseZC,
  title={tRNase Z catalysis and conserved residues on the carboxy side of the His cluster.},
  author={Shay Karkashon and Angela Hopkinson and Louis Levinger},
  journal={Biochemistry},
  year={2007},
  volume={46 33},
  pages={9380-7}
}
tRNAs are transcribed as precursors and processed in a series of required reactions leading to aminoacylation and translation. The 3'-end trailer can be removed by the pre-tRNA processing endonuclease tRNase Z, an ancient, conserved member of the beta-lactamase superfamily of metal-dependent hydrolases. The signature sequence of this family, the His domain (HxHxDH, Motif II), and histidines in Motifs III and V and aspartate in Motif IV contribute seven side chains for the coordination of two… CONTINUE READING
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