Structure of the 30S ribosomal subunit

Nature. 2000 Sep 21;407(6802):327-39. doi: 10.1038/35030006.

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 A 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Crystallography, X-Ray
  • Macromolecular Substances
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Conformation
  • RNA, Bacterial / chemistry
  • RNA, Ribosomal / chemistry*
  • Ribosomal Proteins / chemistry*
  • Ribosomes / chemistry*
  • Thermus thermophilus

Substances

  • Bacterial Proteins
  • Macromolecular Substances
  • RNA, Bacterial
  • RNA, Ribosomal
  • Ribosomal Proteins

Associated data

  • PDB/1FJF