Solution structure of the natively assembled yeast ribosomal stalk determined by small-angle X-ray scattering
Copyright policy )Solution structure of the natively assembled yeast ribosomal stalk determined by small-angle X-ray scattering
The ribosomal stalk of the 60S subunit has been shown to play a crucial role in all steps of protein synthesis, but its structure and exact molecular function remain an unanswered question. In the present study, we show the low-resolution models of the solution structure of the yeast ribosomal stalk, composed of five proteins, P0–(P1–P2)2. The model of the pentameric stalk complex determined by small-angle X-ray scattering reveals an elongated shape with a maximum length of 13 nm. The model displays three distinct lobes, which may correspond to the individual P1–P2 heterodimers anchored to the C-terminal domain of the P0 protein.
Ribosomal Proteins, Saccharomyces cerevisiae Proteins, info:eu-repo/classification/ddc/540, Saccharomyces cerevisiae Proteins: chemistry, Protein Binding: physiology, Saccharomyces cerevisiae, Protein Structure, Tertiary, X-Ray Diffraction: methods, X-Ray Diffraction, Scattering, Small Angle, RPP0 protein, S cerevisiae, ribosomal protein P0, Saccharomyces cerevisiae: chemistry, Protein Multimerization, Ribosomal Proteins: chemistry, Protein Binding
Ribosomal Proteins, Saccharomyces cerevisiae Proteins, info:eu-repo/classification/ddc/540, Saccharomyces cerevisiae Proteins: chemistry, Protein Binding: physiology, Saccharomyces cerevisiae, Protein Structure, Tertiary, X-Ray Diffraction: methods, X-Ray Diffraction, Scattering, Small Angle, RPP0 protein, S cerevisiae, ribosomal protein P0, Saccharomyces cerevisiae: chemistry, Protein Multimerization, Ribosomal Proteins: chemistry, Protein Binding
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