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

• Published in: Cell 2006-09, Vol.126 (6), p.1065-1077
• Main Authors: Korostelev, Andrei, Trakhanov, Sergei, Laurberg, Martin, Noller, Harry F.
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - biosynthesis; Crystallography, X-Ray; Macromolecular Substances - chemistry; Nucleic Acid Conformation; Ribosomes - chemistry; Ribosomes - genetics; RNA, Messenger - chemistry; RNA, Messenger - genetics; RNA, Ribosomal - chemistry; RNA, Ribosomal - genetics; RNA, Transfer - chemistry; RNA, Transfer - genetics; Thermus thermophilus; Thermus thermophilus - genetics; Thermus thermophilus - metabolism
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/j.cell.2006.08.032

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 Å 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.