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, 126 (6), 1065-77

Crystal Structure of a 70S ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements

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Crystal Structure of a 70S ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements

Andrei Korostelev et al. Cell.

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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