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- W2023200543 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 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." @default.
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- W2023200543 date "1998-05-01" @default.
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- W2023200543 title "Ribonuclease P Protein Structure: Evolutionary Origins in the Translational Apparatus" @default.
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- W2023200543 doi "https://doi.org/10.1126/science.280.5364.752" @default.
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