Structural elucidation of substrate-bound aminoglycoside acetyltransferase (3)-IIIa.

Structural elucidation of substrate-bound aminoglycoside acetyltransferase (3)-IIIa.

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Canonical aminoglycosides are a large group of antibiotics, where the part of chemical diversity stems from the substitution of the neamine ring system on positions 5 and 6.Certain aminoglycoside modifying enzymes can modify a broad range of 4,5- and 4,6-disubstituted aminoglycosides, with some as many as 15.This study presents the structural and kinetic results describing a promiscuous aminoglycoside serra avatar price acetyltransferase AAC(3)-IIIa.This enzyme has been crystallized in ternary complex with coenzyme A and 4,5- and 4,6-disubstituted aminoglycosides.

We have followed up this work with kinetic characterization utilizing a panel of diverse aminoglycosides, including a next-generation aminoglycoside, plazomicin.Lastly, we observed an alternative binding mode of gentamicin in the aminoglycoside binding site, which was proven to 15-eg1053cl be a crystallographic artifact based on mutagenesis.