Crystallization and preliminary X-ray crystallographic analysis of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa

Authors: Kim, Hye-Lee; Yoon, Hye-Jin; Ha, Jun Yong; Lee, Byung Il; Lee, Hyung Ho; Mikami, Bunzo; Suh, Se Won

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 948-949(2)

Publisher: Blackwell Publishing

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Abstract:

The enzyme nicotinic acid mononucleotide adenylyltransferase (NaMN AT; EC 2.7.7.18) is essential for the synthesis of nicotinamide adenine dinucleotide and is a potential target for antibiotics. It catalyzes the transfer of an adenyl group from ATP to nicotinic acid mononucleotide to form nicotinic acid adenine dinucleotide. NaMN AT from Pseudomonas aeruginosa was overexpressed in Escherichia coli and crystallized at 291 K using 100 mM bis-Tris propane pH 7.0, 700 mM trisodium citrate and 15%(v/v) glycerol. X-ray diffraction data have been collected to 1.70 Å. The crystals are tetragonal, belonging to space group P4₁22 (or P4₃22), with unit-cell parameters a = b = 65.02, c = 109.80 Å. The presence of one monomer in the asymmetric unit gives a reasonable V_M of 2.15 Å³ Da⁻¹, with a solvent content of 42.7%.

Keywords: nadD; nicotinamide adenine dinucleotide; nicotinic acid mononucleotide; nicotinic acid mononucleotide adenylyltransferase; Pseudomonas aeruginosa

Document Type: Research article

DOI: 10.1107/S0907444904005591

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