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Structure of the 30S ribosomal subunit

Wimberly, Brian T. and Brodersen, Ditlev E. and Clemons, William M., Jr. and Morgan-Warren, Robert J. and Carter, Andrew P. and Vonrhein, Clemens and Hartsch, Thomas and Ramakrishnan, V. (2000) Structure of the 30S ribosomal subunit. Nature, 407 (6802). pp. 327-339. ISSN 0028-0836. https://resolver.caltech.edu/CaltechAUTHORS:20181030-134119080

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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.


Item Type:Article
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URLURL TypeDescription
https://doi.org/10.1038/35030006DOIArticle
https://rdcu.be/bapq0PublisherFree ReadCube access
ORCID:
AuthorORCID
Clemons, William M., Jr.0000-0002-0021-889X
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.
Funders:
Funding AgencyGrant Number
Medical Research Council (UK)UNSPECIFIED
NIH Predoctoral FellowshipUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
European Molecular Biology Organization (EMBO)UNSPECIFIED
Issue or Number:6802
Record Number:CaltechAUTHORS:20181030-134119080
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20181030-134119080
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:90508
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:31 Oct 2018 14:10
Last Modified:03 Oct 2019 20:25

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