Structure of the 30S ribosomal subunit

Brian T. Wimberly, Ditlev E. Brodersen, William M. Clemons, Robert J. Morgan-Warren, Andrew P. Carter, Clemens Vonrhein, Thomas Hartsch and V. Ramakrishnan ()
Additional contact information
Brian T. Wimberly: MRC Laboratory of Molecular Biology
Ditlev E. Brodersen: MRC Laboratory of Molecular Biology
William M. Clemons: MRC Laboratory of Molecular Biology
Robert J. Morgan-Warren: MRC Laboratory of Molecular Biology
Andrew P. Carter: MRC Laboratory of Molecular Biology
Clemens Vonrhein: Global Phasing Ltd., Sheraton House
Thomas Hartsch: Göttingen Genomics Laboratory, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen
V. Ramakrishnan: MRC Laboratory of Molecular Biology

Nature, 2000, vol. 407, issue 6802, 327-339

Abstract: Abstract Genetic information encoded in messenger RNA is translated into protein by the ribosome, which is a large nucleoprotein complex comprising two subunits, denoted 30S and 50S in bacteria. Here we report the crystal structure of the 30S subunit from Thermus thermophilus, refined to 3 Å resolution. The final atomic model rationalizes over four decades of biochemical data on the ribosome, and provides a wealth of information about RNA and protein structure, protein–RNA interactions and ribosome assembly. It is also a structural basis for analysis of the functions of the 30S subunit, such as decoding, and for understanding the action of antibiotics. The structure will facilitate the interpretation in molecular terms of lower resolution structural data on several functional states of the ribosome from electron microscopy and crystallography.

Date: 2000
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DOI: 10.1038/35030006

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