Structural basis for the antibiotic activity of ketolides and azalides

Frank Schlünzen, Jörg M. Harms, Francois Franceschi, Harly A.S. Hansen, Heike Bartels, Raz Zarivach, Ada Yonath

Research output: Contribution to journalArticlepeer-review

221 Scopus citations

Abstract

The azalide azithromycin and the ketolide ABT-773, which were derived by chemical modifications of erythromycin, exhibit elevated activity against a number of penicillin- and macrolide-resistant pathogenic bacteria. Analysis of the crystal structures of the large ribosomal subunit from Deinococcus radiodurans complexed with azithromycin or ABT-773 indicates that, despite differences in the number and nature of their contacts with the ribosome, both compounds exert their antimicrobial activity by blocking the protein exit tunnel. In contrast to all macrolides studied so far, two molecules of azithromycin bind simultaneously to the tunnel. The additional molecule also interacts with two proteins, L4 and L22, implicated in macrolide resistance. These studies illuminated and rationalized the enhanced activity of the drugs against specific macrolide-resistant bacteria.

Original languageEnglish
Pages (from-to)329-338
Number of pages10
JournalStructure
Volume11
Issue number3
DOIs
StatePublished - 1 Mar 2003
Externally publishedYes

Keywords

  • Antibiotics
  • Azalides
  • Azithromycin
  • Ketolides
  • Peptidyl transferase center
  • Ribosome

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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