The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance.
Unge, J., berg, A., Al-Kharadaghi, S., Nikulin, A., Nikonov, S., Davydova, N., Nevskaya, N., Garber, M., Liljas, A.(1998) Structure 6: 1577-1586
- PubMed: 9862810 
- DOI: https://doi.org/10.1016/s0969-2126(98)00155-5
- Primary Citation of Related Structures:  
1BXE - PubMed Abstract: 
. 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 regarding the location of L22 on the ribosome.
Organizational Affiliation: 
Molecular Biophysics, Lund University, PO Box 124 221 00 Lund, Sweden.