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

Authors :
Revillo Imbernon, Julia
Weibel, Jean‐Marc
Ennifar, Eric
Prévost, Gilles
Kellenberger, Esther
Source :
Molecular Informatics; Jul2024, Vol. 43 Issue 7, p1-15, 15p
Publication Year :
2024

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
18681743
Volume :
43
Issue :
7
Database :
Complementary Index
Journal :
Molecular Informatics
Publication Type :
Academic Journal
Accession number :
178427094
Full Text :
https://doi.org/10.1002/minf.202300339