Structures of the bacterial ribosome in classical and hybrid states of tRNA binding Academic Article uri icon


MeSH Major

  • RNA, Bacterial
  • RNA, Transfer, Phe
  • Ribosome Subunits, Large, Bacterial
  • Ribosome Subunits, Small, Bacterial


  • During protein synthesis, the ribosome controls the movement of tRNA and mRNA by means of large-scale structural rearrangements. We describe structures of the intact bacterial ribosome from Escherichia coli that reveal how the ribosome binds tRNA in two functionally distinct states, determined to a resolution of ~3.2 angstroms by means of x-ray crystallography. One state positions tRNA in the peptidyl-tRNA binding site. The second, a fully rotated state, is stabilized by ribosome recycling factor and binds tRNA in a highly bent conformation in a hybrid peptidyl/exit site. The structures help to explain how the ratchet-like motion of the two ribosomal subunits contributes to the mechanisms of translocation, termination, and ribosome recycling.

publication date

  • May 20, 2011



  • Academic Article



  • eng

PubMed Central ID

  • PMC3176341

Digital Object Identifier (DOI)

  • 10.1126/science.1202692

PubMed ID

  • 21596992

Additional Document Info

start page

  • 981

end page

  • 4


  • 332


  • 6032