Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.

@article{Harms2008TranslationalRV,
  title={Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.},
  author={Joerg M. Harms and Daniel N. Wilson and Frank Schluenzen and Sean R Connell and Torsten Stachelhaus and Zaneta Zaborowska and Christian Spahn and Paola Fucini},
  journal={Molecular cell},
  year={2008},
  volume={30 1},
  pages={26-38}
}
The thiopeptide class of antibiotics targets the GTPase-associated center (GAC) of the ribosome to inhibit translation factor function. Using X-ray crystallography, we have determined the binding sites of thiostrepton (Thio), nosiheptide (Nosi), and micrococcin (Micro), on the Deinococcus radiodurans large ribosomal subunit. The thiopeptides, by binding within a cleft located between the ribosomal protein L11 and helices 43 and 44 of the 23S rRNA, overlap with the position of domain V of EF-G… CONTINUE READING

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Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain

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