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Publication Abstract from PubMed

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 betaalphabeta 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.

Ribonuclease P protein structure: evolutionary origins in the translational apparatus.,Stams T, Niranjanakumari S, Fierke CA, Christianson DW Science. 1998 May 1;280(5364):752-5. PMID:9563955^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.