Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; the aminoglycoside phosphotransferase(3')-IIIa

Date

2010-04-01

Author

Serpersu, Engin H.
Özen, Can
Norris, Adrianne L.
Steren, Carlos
Whittemore, Neil

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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 similar to 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 similar to 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 (C alpha, C, N, H, and some C beta) of this protein (BMRB-16337).

Subject Keywords

Antibiotic Resistance, Aminoglycoside, Phosphotransferase, Backbone Resonance, Assignments, Promiscuous Enzyme

URI

https://hdl.handle.net/11511/31324

Journal

BIOMOLECULAR NMR ASSIGNMENTS

DOI

https://doi.org/10.1007/s12104-009-9195-z

Collections

Graduate School of Natural and Applied Sciences, Article

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Citation Formats

E. H. Serpersu, C. Özen, A. L. Norris, C. Steren, and N. Whittemore, “Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; the aminoglycoside phosphotransferase(3′)-IIIa,” BIOMOLECULAR NMR ASSIGNMENTS, pp. 9–12, 2010, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/31324.