1j5a

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spinqualitylabelsall models 1j5a, resolution 3.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL BASIS FOR THE INTERACTION OF ANTIBIOTICS WITH THE PEPTIDYL TRANSFERASE CENTER IN EUBACTERIA

Overview

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.

About this Structure

1J5A is a Protein complex structure of sequences from Deinococcus radiodurans with CTY and MG as ligands. This structure superseeds the now removed PDB entry 1K00. Full crystallographic information is available from OCA.

Reference

Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria., Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F, Nature. 2001 Oct 25;413(6858):814-21. PMID:11677599

Page seeded by OCA on Tue Nov 20 17:56:52 2007