Report

Ribonuclease P Protein Structure: Evolutionary Origins in the Translational Apparatus

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Science  01 May 1998:
Vol. 280, Issue 5364, pp. 752-755
DOI: 10.1126/science.280.5364.752

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Abstract

The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalytic activity. Mutagenesis and biochemical data indicate that an unusual left-handed βαβ crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.

  • * To whom correspondence should be addressed. E-mail: chris{at}xtal.chem.upenn.edu

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