1bxe
From Proteopedia
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RIBOSOMAL PROTEIN L22 FROM THERMUS THERMOPHILUS
Overview
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 regarding, the location of L22 on the ribosome. Results:. The structure of Thermus, thermophilus L22 was solved using X-ray crystallography. L22 consists of a, small alpha+beta domain and a protruding beta hairpin that is 30 A long. A, large part of the surface area of the protein has the potential to be, involved in interactions with rRNA. A structural similarity to other, RNA-binding proteins is found, possibly indicating a common evolutionary, origin. Conclusions:. The extensive surface area of L22 has the, characteristics of an RNA-binding protein, consistent with its role in the, folding of the 23S rRNA. The erythromycin-resistance conferring mutation, is located in the protruding beta hairpin that is postulated to be, important in L22-rRNA interactions. This region of the protein might be at, the erythromycin-binding site close to the peptidyl transferase center, whereas the opposite end may be exposed to the cytoplasm.
About this Structure
1BXE is a Single protein structure of sequence from Thermus thermophilus with CL as ligand. Full crystallographic information is available from OCA.
Reference
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, Structure. 1998 Dec 15;6(12):1577-86. PMID:9862810
Page seeded by OCA on Tue Nov 20 11:59:50 2007
