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

https://www.ncbi.nlm.nih.gov/pubmed/38853661

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.