7bxz

Publication Abstract from PubMed

Aminoglycoside acetyltransferases (AACs) catalyze the transfer of an acetyl group between acetyl-CoA and an aminoglycoside, producing CoA and an acetylated aminoglycoside. AAC(6')-Ii enzymes target the amino group linked to the 6' C atom in an aminoglycoside. Several structures of the AAC(6')-Ii from Enterococcus faecium [Ef-AAC(6')-Ii] have been reported to date. However, the detailed mechanism of its enzymatic function remains elusive. In this study, the crystal structure of Ef-AAC(6')-Ii was determined in a novel substrate-free form. Based on structural analysis, it is proposed that Ef-AAC(6')-Ii sequentially undergoes conformational selection and induced fit for substrate binding. These results therefore provide a novel viewpoint on the mechanism of action of Ef-AAC(6')-Ii.

Structural analysis of a novel substrate-free form of the aminoglycoside 6'-N-acetyltransferase from Enterococcus faecium.,Jang H, Kwon S, Jeong CS, Lee CW, Hwang J, Jung KH, Lee JH, Park HH Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):364-371. doi:, 10.1107/S2053230X20009735. Epub 2020 Jul 28. PMID:32744248^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.