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Science 1 May 1998:
Vol. 280. no. 5364, pp. 752 - 755
DOI: 10.1126/science.280.5364.752
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Reports

Ribonuclease P Protein Structure: Evolutionary Origins in the Translational Apparatus

Travis Stams, S. Niranjanakumari, Carol A. Fierke, David W. Christianson *

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 beta alpha beta 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.

T. Stams and D. W. Christianson, Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
S. Niranjanakumari and C. A. Fierke, Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
*   To whom correspondence should be addressed. E-mail: chris{at}xtal.chem.upenn.edu

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