Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements

Cell. 2006 Sep 22;126(6):1065-77. doi: 10.1016/j.cell.2006.08.032. Epub 2006 Sep 7.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / biosynthesis*
  • Crystallography, X-Ray
  • Macromolecular Substances / chemistry
  • Nucleic Acid Conformation
  • RNA, Messenger / chemistry*
  • RNA, Messenger / genetics
  • RNA, Ribosomal / chemistry*
  • RNA, Ribosomal / genetics
  • RNA, Transfer / chemistry*
  • RNA, Transfer / genetics
  • Ribosomes / chemistry*
  • Ribosomes / genetics
  • Thermus thermophilus / genetics*
  • Thermus thermophilus / metabolism


  • Bacterial Proteins
  • Macromolecular Substances
  • RNA, Messenger
  • RNA, Ribosomal
  • RNA, Transfer