The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance.

@article{Unge1998TheCS,
  title={The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance.},
  author={Jeannette Unge and Albrecht Berg and S Al-Kharadaghi and Alexei Nikulin and Stanislav Nikonov and Natalia Davydova and Natalia Nevskaya and Maria Garber and Anders Liljas},
  journal={Structure},
  year={1998},
  volume={6 12},
  pages={
          1577-86
        }
}
BACKGROUND . The ribosomal protein L22 is one of five proteins necessary for the formation of an early folding intermediate of the 23S rRNA. L22 has been found on the cytoplasmic side of the 50S ribosomal subunit. It can also be labeled by an erythromycin derivative bound close to the peptidyl-transfer center at the interface side of the 50S subunit, and the amino acid sequence of an erythromycin-resistant mutant is known. Knowing the structure of the protein may resolve this apparent conflict… CONTINUE READING
Highly Cited
This paper has 17 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-8 of 8 citations