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Structural analysis of neomycin B and kanamycin A binding Aminoglycosides Modifying Enzymes (AME) and bacterial ribosomal RNA.

Julia Revillo ImbernonJean-Marc WeibelEric EnnifarGilles PrévostEsther Kellenberger
Published in: Molecular informatics (2024)
Aminoglycosides are crucial antibiotics facing challenges from bacterial resistance. This study addresses the importance of aminoglycoside modifying enzymes in the context of escalating resistance. Drawing upon over two decades of structural data in the Protein Data Bank, we focused on two key antibiotics, neomycin B and kanamycin A, to explore how the aminoglycoside structure is exploited by this family of enzymes. A systematic comparison across diverse enzymes and the RNA A-site target identified common characteristics in the recognition mode, while assessing the adaptability of neomycin B and kanamycin A in various environments.
Keyphrases
  • electronic health record
  • pseudomonas aeruginosa
  • big data
  • acinetobacter baumannii
  • binding protein
  • machine learning
  • nucleic acid