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  • Title: Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements.
    Author: Korostelev A, Trakhanov S, Laurberg M, Noller HF.
    Journal: Cell; 2006 Sep 22; 126(6):1065-77. PubMed ID: 16962654.
    Abstract:
    Our understanding of the mechanism of protein synthesis has undergone rapid progress in recent years as a result of low-resolution X-ray and cryo-EM structures of ribosome functional complexes and high-resolution structures of ribosomal subunits and vacant ribosomes. Here, we present the crystal structure of the Thermus thermophilus 70S ribosome containing a model mRNA and two tRNAs at 3.7 A resolution. Many structural details of the interactions between the ribosome, tRNA, and mRNA in the P and E sites and the ways in which tRNA structure is distorted by its interactions with the ribosome are seen. Differences between the conformations of vacant and tRNA-bound 70S ribosomes suggest an induced fit of the ribosome structure in response to tRNA binding, including significant changes in the peptidyl-transferase catalytic site.
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