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Crystallization and preliminary crystallographic analysis of hygromycin B phosphotransferase from Escherichia coli

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Aminoglycoside antibiotics, such as hygromycin, kanamycin, neomycin, spectinomycin and streptomycin, inhibit protein synthesis by acting on bacterial and eukaryotic ribosomes. Hygromycin B phosphotransferase (Hph; EC converts hygromycin B to 7′′‐O‐phosphohygromycin using a phosphate moiety from ATP, resulting in the loss of its cell‐killing activity. The Hph protein has been crystallized for the first time using a thermostable mutant and the hanging‐drop vapour‐diffusion method. The crystal provided diffraction data to a resolution of 2.1 Å and belongs to space group P3221, with unit‐cell parameters a = b = 71.0, c = 125.0 Å. Crystals of complexes of Hph with hygromycin B and AMP‐PNP or ADP have also been obtained in the same crystal form as that of the apoprotein.
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Keywords: MAD; aminoglycoside antibiotics; hygromycin B phosphotransferase; selenomethionine

Document Type: Research Article

Publication date: August 1, 2007

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