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

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2006.08.032 Byline: Andrei Korostelev (1), Sergei Trakhanov (1), Martin Laurberg (1), Harry F. Noller (1) 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. Author Affiliation: (1) Center for Molecular Biology of RNA and Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064, USA Article History: Received 13 July 2006; Revised 10 August 2006; Accepted 30 August 2006 Article Note: (miscellaneous) Published online: September 7, 2006