Structures of the Bacterial Ribosome in Classical and Hybrid States of tRNA Binding
- 20 May 2011
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 332 (6032), 981-984
- https://doi.org/10.1126/science.1202692
Abstract
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.Keywords
Funding Information
- National Cancer Institute (CA92584)
- National Institutes of Health (GM65050, GM079238, GM074127-04S1, GM088674, P01-GM63210, GM07739)
- U.S. Department of Energy (DE-AC03 76SF00098, DE-AC02-06CH11357)
- National Center for Research Resources (RR-15301)
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