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Related Experiment Videos

Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.

Holger Stark1, Marina V Rodnina, Hans-Joachim Wieden

  • 1Max-Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. holger.stark@mpibpc.mpg.de

Nature Structural Biology
|October 16, 2002
PubMed
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This study reveals the ribosome

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Aminoacyl-tRNA (aa-tRNA) binding to the ribosome's A-site is crucial for protein synthesis.
  • This recognition involves a ternary complex of aa-tRNA, elongation factor Tu (EF-Tu), and GTP.

Purpose of the Study:

  • To elucidate the structural basis of codon recognition by the ternary complex at the ribosome.
  • To provide a high-resolution structural snapshot of this key functional state.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine a 3D reconstruction.
  • The reconstruction was performed at 13 Å resolution of a kirromycin-stalled codon-recognition complex.

Main Results:

  • The ternary complex structure is notably distorted upon tRNA anticodon arm binding in the decoding center.

Related Experiment Videos

  • Detailed interactions were observed between aa-tRNA, ribosomal RNA (16S and 23S), and ribosomal proteins (S12, L11).
  • The sarcin-ricin loop of 23S rRNA was found to contact EF-Tu's domain 1.

    • Conclusions:

    • The findings offer a detailed structural view of the ribosome during codon recognition.
    • These insights suggest mechanisms underlying tRNA selection and GTPase activation by EF-Tu.