Science Article Provides Insights About Ribosome

Protein biosynthesis occurs on the ribosome in all forms of life.

The Science

Lawrence Berkeley National Laboratory researcher Dr. James Cate and collaborators provided important new insights into the operation of the ribosome, the molecular complex that manufactures proteins in the cell. Using x-ray crystallography, Dr. Cate and his colleagues determined two high resolution ribosome crystal structures resulting in the first detailed view of the interface between ribosome subunits as well as its center for producing proteins. These structures provide a detailed view of the interface between the small and large ribosomal subunits and the conformation of the peptidyl transferase center in the context of the intact ribosome. Differences between the two ribosomes reveal a high degree of flexibility between the head and the rest of the small subunit. Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA (mRNA) and transfer RNAs (tRNAs) during translocation. The research is part of the Genomics:GTL effort to develop strategies to label complexes to track their operation in microbial cells.


The National Institutes of Health partially supported this work.


Schuwirth, B. S., M. A. Borovinskaya, C. W. Hau, W. Zhang, A. Vila-Sanjurjo, J. M. Holton, and J. H. Doudna Cate. 2005. “Structures of the Bacterial Ribosome at 3.5 Å Resolution,” Science 310, 827–34. DOI:10.1126/science.1117230.