Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria

Frank Schlünzen, Raz Zarivach, Jörg Harms, Anat Bashan, Ante Tocilj, Renate Albrecht, Ada Yonath and François Franceschi ()
Additional contact information
Frank Schlünzen: Max-Planck-Research, Unit for Ribosomal Structure
Raz Zarivach: Weizmann Institute
Jörg Harms: Max-Planck-Research, Unit for Ribosomal Structure
Anat Bashan: Weizmann Institute
Ante Tocilj: Max-Planck-Research, Unit for Ribosomal Structure
Renate Albrecht: Max-Planck-Institut für Molekulare Genetik
Ada Yonath: Max-Planck-Research, Unit for Ribosomal Structure
François Franceschi: Max-Planck-Institut für Molekulare Genetik

Nature, 2001, vol. 413, issue 6858, 814-821

Abstract: 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.

Date: 2001
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/35101544 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:413:y:2001:i:6858:d:10.1038_35101544

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/35101544

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().