| Home > Publications database > Solution structure of natively assembled yeast ribosomal stalk determined by Small Angle X-ray Scattering |
| Journal Article | PHPPUBDB-24926 |
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2012
Portland Press
London
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Please use a persistent id in citations: doi:10.1042/BJ20120115
Abstract: 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.
Keyword(s): Protein Binding: physiology (MeSH) ; Protein Multimerization (MeSH) ; Protein Structure, Tertiary (MeSH) ; Ribosomal Proteins: chemistry (MeSH) ; Saccharomyces cerevisiae: chemistry (MeSH) ; Saccharomyces cerevisiae Proteins: chemistry (MeSH) ; Scattering, Small Angle (MeSH) ; X-Ray Diffraction: methods (MeSH) ; RPP0 protein, S cerevisiae ; Ribosomal Proteins ; Saccharomyces cerevisiae Proteins ; ribosomal protein P0
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