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 βαβ crosso...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1998-05, Vol.280 (5364), p.752-755
Hauptverfasser:	Stams, Travis, Niranjanakumari, S., Fierke, Carol A., Christianson, David W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Bacillus subtilis - enzymology Bacteria Binding Sites Binding sites (Biochemistry) Biochemistry Biological and medical sciences Catalysis Crossovers Crystal structure Crystallography, X-Ray Crystals Endoribonucleases - chemistry Endoribonucleases - metabolism Enzymes and enzyme inhibitors Evolution Evolution, Molecular Fundamental and applied biological sciences. Psychology Hydrolases Literary Devices Magnesium - metabolism Metal ions Models, Molecular Peptide Elongation Factor G Peptide Elongation Factors - chemistry Protein Biosynthesis Protein Conformation Protein Folding Protein Structure, Secondary Protein subunits Proteins Ribonuclease Ribonuclease P Ribonucleic acid Ribosomal Proteins - chemistry RNA RNA, Bacterial - chemistry RNA, Bacterial - metabolism RNA, Catalytic - chemistry RNA, Catalytic - metabolism Topology Zinc - metabolism
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