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 ZN and SO4 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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