U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome.

@article{Grel2009U2504DT,
  title={U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome.},
  author={G{\"u}liz G{\"u}rel and Gregor M. Blaha and Peter B Moore and Thomas A Steitz},
  journal={Journal of molecular biology},
  year={2009},
  volume={389 1},
  pages={146-56}
}
Structures have been obtained for the complexes that tiamulin, homoharringtonine, and bruceantin form with the large ribosomal subunit of Haloarcula marismortui at resolutions ranging from 2.65 to 3.2 A. They show that all these inhibitors block protein synthesis by competing with the amino acid side chains of incoming aminoacyl-tRNAs for binding in the A-site cleft in the peptidyl-transferase center, which is universally conserved. In addition, these structures support the hypothesis that the… CONTINUE READING

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