Structure of the bifunctional aminoglycoside-resistance enzyme AAC(6′)-Ie-APH(2′′)-Ia revealed by crystallographic and small-angle X-ray scattering analysis

The X-ray structure of the N-terminal acetyltransferase domain [AAC(6′)-Ie] of the bifunctional antibiotic-resistance enzyme AAC(6′)-Ie-APH(2′′)-Ia has been determined as a ternary kanamycin/coenzyme A complex. X-ray structures of the isolated AAC(6′)-Ie and APH(2′′)-Ia domains, combined with small-angle X-ray scattering (SAXS) data, allowed the determination of the structural architecture of the full-length bifunctional enzyme in solution.

Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia

The crystal structure of the C-terminal phosphotransferase domain of the bifunctional aminoglycoside acetyltransferase-phosphotransferase AAC(6')-Ie-APH(2'')-Ia has been determined to 2.3 Å resolution. The enzyme was crystallized as the Mg₂GDP binary complex.