Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; the aminoglycoside phosphotransferase(3')-IIIa.
The aminoglycoside phosphotransferase(3')-IIIa (APH) is a promiscuous enzyme and renders a large number of structurally diverse aminoglycoside antibiotics useless against infectious bacteria. A remarkable property of this approximately 31 kDa enzyme is in its unusual dynamic behavior in solution; the apo-form of the enzyme exchanges all of its backbone amide protons within 15 h of exposure to D ( 2 ) O while aminoglycoside-bound forms retain approximately 40% of the amide protons even after >90 h of exposure. Moreover, the number of observable peaks and their dispersion in HSQC spectra varies with each aminoglycoside, rendering the resonance assignments very challenging. Therefore, the binary APH-tobramycin complex, which shows the largest number of well-resolved peaks, was used for the backbone resonance assignments (Calpha, C, N, H, and some Cbeta) of this protein (BMRB-16337).
Serpersu
Engin H
EH
Department of Biochemistry Cellular and Molecular Biology, The University of Tennessee, Knoxville, TN 37996, USA. serpersu@utk.edu
Ozen
Can
C
Norris
Adrianne L
AL
Steren
Carlos
C
Whittemore
Neil
N
D001426:Bacterial Proteins / Q000737:chemistry; D006801:Humans; D019868:Kanamycin Kinase / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular
D001426:Bacterial Proteins; D019868:Kanamycin Kinase