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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacillus subtilis / enzymology
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Binding Sites
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Catalysis
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Crystallography, X-Ray
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Endoribonucleases / chemistry*
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Endoribonucleases / metabolism
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Evolution, Molecular*
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Magnesium / metabolism
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Models, Molecular
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Peptide Elongation Factor G
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Peptide Elongation Factors / chemistry
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Protein Biosynthesis*
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Protein Conformation*
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Protein Folding
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Protein Structure, Secondary
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RNA, Bacterial / chemistry*
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RNA, Bacterial / metabolism
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RNA, Catalytic / chemistry*
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RNA, Catalytic / metabolism
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Ribonuclease P
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Ribosomal Proteins / chemistry
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Zinc / metabolism
Substances
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Peptide Elongation Factor G
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Peptide Elongation Factors
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RNA, Bacterial
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RNA, Catalytic
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Ribosomal Proteins
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ribosomal protein S5
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Endoribonucleases
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Ribonuclease P
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Magnesium
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Zinc