1BXE

RIBOSOMAL PROTEIN L22 FROM THERMUS THERMOPHILUS

Summary for 1BXE

• Entry DOI: 10.2210/pdb1bxe/pdb
• Descriptor: PROTEIN (RIBOSOMAL PROTEIN L22), CHLORIDE ION (3 entities in total)
• Functional Keywords: ribosomal protein, protein synthesis, rna binding, antibiotics resistance, rna binding protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 13008.20

Authors

Unge, J.,Aberg, A.,Al-Karadaghi, S.,Nikulin, A.,Nikonov, S.,Davydova, N.,Nevskaya, N.,Garber, M.,Liljas, A. (deposition date: 1998-10-02, release date: 1998-10-07, Last modification date: 2024-10-30)

Primary citation

Unge, J.,berg, A.,Al-Kharadaghi, S.,Nikulin, A.,Nikonov, S.,Davydova, N.,Nevskaya, N.,Garber, M.,Liljas, A.
The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance.
Structure, 6:1577-1586, 1998

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.

PubMed: 9862810
DOI: 10.1016/S0969-2126(98)00155-5

Experimental method

X-RAY DIFFRACTION (1.9 Å)