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The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA

Nature volume 358, pages 768–771 (1992)Cite this article

Abstract

UNDERSTANDING the process whereby the ribosome translates the genetic code into protein molecules will ultimately require high-resolution structural information, and we report here the first crystal structure of a protein from the small ribosomal subunit. This protein, S5, has a molecular mass of 17,500 and is highly conserved in all lifeforms1–4. The molecule contains two distinct α/β domains that have structural similarities to several other proteins that are components of ribonucleoprotein complexes. Mutations in S5 result in several phenotypes which suggest that S5 may have a role in translational fidelity and translocation. These include ribosome ambiguity or ram5, reversion from streptomycin dependence6 and resistance to spectinomycin6. Also, a cold-sensitive, spectinomycin-resistant mutant of S5 has been identified which is defective in initiation7. Here we show that these mutations map to two distinct regions of the molecule which seem to be sites of interaction with ribosomal RNA. A structure/function analysis of the molecule reveals discrepancies with current models8,9 of the 308 subunit.

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Authors and Affiliations

  1. Biology Department, Brookhaven National Laboratory, Upton, New York, 11973, USA

    V. Ramakrishnan

  2. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    V. Ramakrishnan

  3. Department of Microbiology, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Stephen W. White

Authors
  1. V. Ramakrishnan
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  2. Stephen W. White
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Ramakrishnan, V., White, S. The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA. Nature 358, 768–771 (1992). https://doi.org/10.1038/358768a0

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