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Published Online March 29, 2001
Science DOI: 10.1126/science.1060089

Research Articles

Submitted on February 21, 2001
Accepted on March 20, 2001

Crystal Structure of the Ribosome at 5.5 Å Resolution

Marat M. Yusupov 1*, Gulnara Zh. Yusupova 1, Albion Baucom 2, Kate Lieberman 2, Thomas N. Earnest 3, J. H. D. Cate 4*, Harry F. Noller 2*

1 Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California at Santa Cruz, Santa Cruz, CA, 95064, USA; UPR 9004 de Biologie et de Genomiques Structurales du CNRS, IGBMC B.P. 163, 1 rue L.Fries, 67404 Illkirch Cedex - CU de Strasbourg, France.
2 Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California at Santa Cruz, Santa Cruz, CA, 95064, USA.
3 Berkeley Center for Structural Biology, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
4 Whitehead Institute, Cambridge, MA, 01242, USA.

We describe the crystal structure of the complete Thermus thermophilus 70S ribosome containing bound mRNA and tRNAs at 5.5 Å resolution. All of the 16S, 23S and 5S rRNA chains, the A-, P- and E-site tRNAs, and most of the ribosomal proteins can be fitted to the electron density map. The core of the interface between the 30S small subunit and the 50S large subunit, where the tRNA substrates are bound, is dominated by RNA, with proteins located mainly at the periphery, consistent with ribosomal function being based on rRNA. In each of the three tRNA binding sites, the ribosome contacts all of the major elements of tRNA, providing an explanation for the conservation of tRNA structure. The tRNAs are closely juxtaposed with the intersubunit bridges, in a way that suggests coupling of the 20 to 50 Å movements associated with tRNA translocation with intersubunit movement.


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