Structural analysis of neomycin B and kanamycin A binding Aminoglycosides Modifying Enzymes (AME) and bacterial ribosomal RNA.
Fiche publication
Date publication
juin 2024
Journal
Molecular informatics
Auteurs
Membres identifiés du Cancéropôle Est :
Dr ENNIFAR Eric
Tous les auteurs :
Revillo Imbernon J, Weibel JM, Ennifar E, Prévost G, Kellenberger E
Lien Pubmed
Résumé
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.
Mots clés
aminoglycoside N-Acetyltransferase, aminoglycoside O-Nucleotidyltransferase, aminoglycoside O-Phosphotransferase, binding mode, interactions
Référence
Mol Inform. 2024 06 10;:e202300339