Crystal structures of the bacterial ribosomal decoding site complexed with amikacin containing the gamma-amino-alpha-hydroxybutyrl (haba) group

J Kondo, B Francois, Rupert James Martin Russell, JB Murray, E Westhof

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

Abstract

Amikacin is the 4,6-linked aminoglycoside modified at position N1 of the 2-deoxystreptamine ring (ring II) by the L-haba group. In the present study, the crystal structure of a complex between oligonucleotide containing the bacterial ribosomal A site and amikacin has been solved at 2.7 angstrom resolution. Amikacin specifically binds to the A site in practically the same way as its parent compound kanamycin. In addition, the L-haba group interacts with the upper side of the A site through two direct contacts, O2*...H-N4(C1496) and N4*-H...O6(G1497). The present crystal structure shows how the introduction of the L-haba group on ring II of aminoglycoside is an effective mutation for obtaining a higher affinity to the bacterial A site. (c) 2006 Published by Elsevier SAS.

Original languageEnglish
Pages (from-to)1027-1031
Number of pages5
JournalBiochimie
Volume88
DOIs
Publication statusPublished - Aug 2006

Keywords

  • aminoglycoside
  • haba group
  • ribosomal decoding site
  • x-ray analysis
  • TRANSFER-RNA
  • CRYSTALLOGRAPHY
  • ANTIBIOTICS
  • SUBUNIT
  • AMINOGLYCOSIDES
  • OLIGONUCLEOTIDE
  • INSIGHTS
  • BINDING

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