1A6F

RNASE P PROTEIN FROM BACILLUS SUBTILIS

Summary for 1A6F

• Entry DOI: 10.2210/pdb1a6f/pdb
• Descriptor: RIBONUCLEASE P PROTEIN, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: endonuclease, rnase, subunit
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 14381.43

Authors

Stams, T.,Christianson, D.W. (deposition date: 1998-02-24, release date: 1999-03-23, Last modification date: 2024-02-07)

Primary citation

Stams, T.,Niranjanakumari, S.,Fierke, C.A.,Christianson, D.W.
Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
Science, 280:752-755, 1998

PubMed 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.

PubMed: 9563955
DOI: 10.1126/science.280.5364.752

Experimental method

X-RAY DIFFRACTION (2.6 Å)