Structure of the 30S ribosomal subunit

@article{Wimberly2000StructureOT,
  title={Structure of the 30S ribosomal subunit},
  author={Brian T. Wimberly and Ditlev Egeskov Brodersen and William M. Clemons and Robert J. Morgan-Warren and Andrew P. Carter and Clemens Vonrhein and Thomas Hartsch and Venki Ramakrishnan},
  journal={Nature},
  year={2000},
  volume={407},
  pages={327-339}
}
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… Expand
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A crystallographic analysis of the structure of the 30S ribosomal subunit from the bacterium Thermus thermophilus shows double-helical regions of RNA to be identified throughout the subunit, and all seven of the small-subunit proteins of known crystal structure to be positioned in the electron density map. Expand
Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
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The functional implications of the high-resolution 30S crystal structure are described, and details of the interactions between the 30S subunit and its tRNA and mRNA ligands are inferred, which lead to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process. Expand
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