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  Structural basis for the antibiotic activity of ketolides and azalides

Schlunzen, F., Harms, J. M., Franceschi, F., Hansen, H. A. S., Bartels, H., Zarivach, R., et al. (2003). Structural basis for the antibiotic activity of ketolides and azalides. Structure, 11(3), 329-338. doi:10.1016/S0969-2126(03)00022-4.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8AA8-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8AA9-3
Genre: Journal Article
Alternative Title : Structure

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 Creators:
Schlunzen, Frank1, Author
Harms, Joerg M.1, Author
Franceschi, Francois2, Author              
Hansen, Harly A. S.1, Author
Bartels, Heike1, Author
Zarivach, Raz1, Author
Yonath, Ada1, Author
Affiliations:
1Max Planck Society, ou_persistent13              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: ribosome, antibiotics, azithromycin, ketolides, azalides, peptidyl transferase center
 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

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Language(s): eng - English
 Dates: 2003-03
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 194834
ISI: 000181539800013
DOI: 10.1016/S0969-2126(03)00022-4
 Degree: -

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Title: Structure
  Alternative Title : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 11 (3) Sequence Number: - Start / End Page: 329 - 338 Identifier: ISSN: 0969-2126