1a6f

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Image:1a6f.gif

1a6f, resolution 2.6Å

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RNASE P PROTEIN FROM BACILLUS SUBTILIS

Overview

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.

About this Structure

1A6F is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Ribonuclease P, with EC number 3.1.26.5 Full crystallographic information is available from OCA.

Reference

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

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