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Related Experiment Videos

Macromolecular mimicry in protein biosynthesis

J Nyborg1, P Nissen, M Kjeldgaard

  • 1Institute of Molecular and Structural Biology, University of Aarhus, Denmark. jnb@kemi.aau.dk

Folding & Design
|January 1, 1997
PubMed
Summary

Elongation factor Tu (EF-Tu), a G-protein crucial for protein synthesis, undergoes significant conformational changes upon GTP binding. These changes enable it to bind aminoacylated tRNAs (aa-tRNAs) and interact with the ribosome.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Elongation factor Tu (EF-Tu) is a G-protein essential for protein biosynthesis.
  • EF-Tu binds and delivers aminoacylated tRNAs (aa-tRNAs) to the ribosome in its GTP-bound state.
  • EF-Tu possesses three structural domains, with switch I and switch II regions sensitive to nucleotide binding.

Purpose of the Study:

  • To investigate the conformational changes of EF-Tu during its functional cycle.
  • To elucidate the structural basis of EF-Tu's interaction with aa-tRNAs.
  • To compare the structure of the EF-Tu.GTP-aa-tRNA ternary complex with other elongation factors.

Main Methods:

  • Structural studies of EF-Tu in its GDP- and GTP-bound forms.
  • Analysis of conformational changes involving switch regions.

Related Experiment Videos

  • Comparison of the ternary complex structure with elongation factor G (EF-G).

    • Main Results:

    • EF-Tu undergoes substantial conformational changes upon activation from EF-Tu.GDP to EF-Tu.GTP.
    • These changes involve rearrangements in switch I and switch II regions, altering domain positions.
    • The ternary complex of EF-Tu.GTP and aa-tRNA shares a similar overall shape with EF-G.

    Conclusions:

    • The structural plasticity of EF-Tu is key to its function in delivering aa-tRNAs.
    • EF-G appears to mimic the tRNA component of the EF-Tu ternary complex.
    • This macromolecular mimicry provides insights into the mechanisms of elongation factors on the ribosome.