Structures of the bacterial ribosome in classical and hybrid states of tRNA binding.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Dunkle, JA; Wang, L; Feldman, MB; Pulk, A; Chen, VB; Kapral, GJ; Noeske, J; Richardson, JS; Blanchard, SC; Cate, JHD

Published Date

  • May 20, 2011

Published In

Volume / Issue

  • 332 / 6032

Start / End Page

  • 981 - 984

PubMed ID

  • 21596992

Pubmed Central ID

  • PMC3176341

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

Digital Object Identifier (DOI)

  • 10.1126/science.1202692


  • eng

Conference Location

  • United States