Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
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.
Stams
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Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Niranjanakumari
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Fierke
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Christianson
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D001412:Bacillus subtilis / Q000201:enzymology; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism; D019143:Evolution, Molecular; D008274:Magnesium / Q000378:metabolism; D008958:Models, Molecular; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000737:chemistry; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012329:RNA, Bacterial / Q000737:chemistry* / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism; D043262:Ribonuclease P; D012269:Ribosomal Proteins / Q000737:chemistry; D015032:Zinc / Q000378:metabolism
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012269:Ribosomal Proteins; C030831:ribosomal protein S5; D004722:Endoribonucleases; D043262:Ribonuclease P; D008274:Magnesium; D015032:Zinc