Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements.
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.
Korostelev
Andrei
A
Center for Molecular Biology of RNA and Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz, CA 95064, USA.
Trakhanov
Sergei
S
Laurberg
Martin
M
Noller
Harry F
HF
D001426:Bacterial Proteins / Q000096:biosynthesis*; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances / Q000737:chemistry; D009690:Nucleic Acid Conformation; D012333:RNA, Messenger / Q000737:chemistry* / Q000235:genetics; D012335:RNA, Ribosomal / Q000737:chemistry* / Q000235:genetics; D012343:RNA, Transfer / Q000737:chemistry* / Q000235:genetics; D012270:Ribosomes / Q000737:chemistry* / Q000235:genetics; D016963:Thermus thermophilus / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D012333:RNA, Messenger; D012335:RNA, Ribosomal; D012343:RNA, Transfer