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  • Title: Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori.
    Author: Eom SJ, Ahn HJ, Kim HW, Baek SH, Suh SW.
    Journal: Acta Crystallogr D Biol Crystallogr; 2003 Mar; 59(Pt 3):561-2. PubMed ID: 12595726.
    Abstract:
    Phosphopantetheine adenylyltransferase (PPAT; EC 2.7.7.3) is an essential enzyme in the coenzyme A (CoA) biosynthetic pathway and catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA. PPAT from Helicobacter pylori has been overexpressed in Escherichia coli and crystallized at 296 K using sodium chloride as a precipitant by the hanging-drop vapour-diffusion method. X-ray diffraction data have been collected to 2.00 A resolution at 100 K using synchrotron radiation. The crystals belong to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 80.50, c = 143.05 A, alpha = beta = 90, gamma = 120 degrees. Six monomers of PPAT are likely to be present in the asymmetric unit, giving a V(M) of 2.39 A(3) Da(-1) and a solvent content of 49%.
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