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Antimicrob Agents Chemother. 2014 Aug;58(8):4308-17. doi: 10.1128/AAC.02857-14. Epub 2014 May 12.

Structural analysis of base substitutions in Thermus thermophilus 16S rRNA conferring streptomycin resistance.

Author information

  • 1Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island, USA.
  • 2NE-CAT/Cornell University, Argonne, Illinois, USA.
  • 3Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island, USA steven_gregory@brown.edu.

Abstract

Streptomycin is a bactericidal antibiotic that induces translational errors. It binds to the 30S ribosomal subunit, interacting with ribosomal protein S12 and with 16S rRNA through contacts with the phosphodiester backbone. To explore the structural basis for streptomycin resistance, we determined the X-ray crystal structures of 30S ribosomal subunits from six streptomycin-resistant mutants of Thermus thermophilus both in the apo form and in complex with streptomycin. Base substitutions at highly conserved residues in the central pseudoknot of 16S rRNA produce novel hydrogen-bonding and base-stacking interactions. These rearrangements in secondary structure produce only minor adjustments in the three-dimensional fold of the pseudoknot. These results illustrate how antibiotic resistance can occur as a result of small changes in binding site conformation.

Copyright © 2014, American Society for Microbiology. All Rights Reserved.

PMID:
24820088
[PubMed - in process]
PMCID:
PMC4136021
Free PMC Article
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