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

Autor:	Zieliński, Michał, Blanchet, Jonathan, Hailemariam, Sophia, Berghuis, Albert M.
Předmět:	ACETYLTRANSFERASES COENZYME A AMINOGLYCOSIDES GENTAMICIN BINDING sites AMIKACIN
Zdroj:	PLoS ONE; 8/3/2022, Vol. 17 Issue 8, p1-14, 14p
Abstrakt:	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 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 be a crystallographic artifact based on mutagenesis. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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