Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published September 21, 2000 | public
Journal Article

Structure of the 30S ribosomal subunit

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.

Additional Information

© 2000 Nature Publishing Group. Received 14 July; accepted 10 August 2000. This work was supported by the Medical Research Council (UK) and a US National Institutes of Health grant to V.R. and S. W. White. Beamlines at Argonne and Brookhaven were supported by the US Department of Energy. D.E.B. was supported by an EMBO long-term postdoctoral fellowship,and W.M.C. by an NIH predoctoral fellowship. We thank B. S. Brunschwig and M. H. Chou for gifts of osmium hexammine and osmium bipyridine; T. Terwilliger for help with phasing using SOLVE; T. A. Leaf-Jones for providing us a version of O with RNA tools; and our colleagues at the LMB for their advice and encouragement. We are indebted to A. Joachimiak, S. L. Ginell, R. Ravelli, S. McSweeney, G. Leonard, A. Thompson, H. Lewis, L. Berman, M. Papiz, S. Girdwood and M. MacDonald for help and advice on synchrotron beamlines.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023