Summary information and primary citation
- PDB-id
-
1j5a;
DSSR-derived features in text and
JSON formats
- Class
- ribosome
- Method
- X-ray (3.5 Å)
- Summary
- Structural basis for the interaction of antibiotics
with the peptidyl transferase center in eubacteria
- Reference
-
Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A,
Albrecht R, Yonath A, Franceschi F (2001): "Structural
basis for the interaction of antibiotics with the
peptidyl transferase centre in eubacteria."
Nature, 413, 814-821. doi:
10.1038/35101544.
- Abstract
- Ribosomes, the site of protein synthesis, are a major
target for natural and synthetic antibiotics. Detailed
knowledge of antibiotic binding sites is central to
understanding the mechanisms of drug action. Conversely,
drugs are excellent tools for studying the ribosome
function. To elucidate the structural basis of
ribosome-antibiotic interactions, we determined the
high-resolution X-ray structures of the 50S ribosomal
subunit of the eubacterium Deinococcus radiodurans,
complexed with the clinically relevant antibiotics
chloramphenicol, clindamycin and the three macrolides
erythromycin, clarithromycin and roxithromycin. We found
that antibiotic binding sites are composed exclusively of
segments of 23S ribosomal RNA at the peptidyl transferase
cavity and do not involve any interaction of the drugs with
ribosomal proteins. Here we report the details of
antibiotic interactions with the components of their
binding sites. Our results also show the importance of
putative Mg+2 ions for the binding of some drugs. This
structural analysis should facilitate rational drug
design.
