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Structures of the Bacterial Ribosome in Classical and Hybrid States of tRNA Binding
- Dunkle, Jack A., Wang, Leyi, Feldman, Michael B., Pulk, Arto, Chen, Vincent B., Kapral, Gary J., Noeske, Jonas, Richardson, Jane S., Blanchard, Scott C., Cate, Jamie H. Doudna
- Science 2011 v.332 no.6032 pp. 981-984
- Escherichia coli, X-ray diffraction, binding sites, messenger RNA, protein subunits, protein synthesis, ribosomal proteins, ribosomes, transfer RNA
- 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 approximately 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.