Izard T, Geerlof A, Lewendon A, Barker J J
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, England.
Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1226-8. doi: 10.1107/s0907444999004394.
Phosphopantetheine adenylyltransferase (PPAT, E.C. 2.7.7.3) catalyzes the penultimate step in coenzyme A (CoA) biosynthesis, transferring an adenylyl group from ATP to 4'-phosphopantetheine, and forming dephospho-CoA. Cubic crystals of native PPAT from Escherichia coli as well as PPAT in complex with its substrates were obtained. The crystals belong to space group I23 or I213 with unit-cell dimension a = 135.5 A. The crystals diffract to better than 1.8 A resolution on a Cu Kalpha rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 2.9 A3 Da-1.
磷酸泛酰巯基乙胺腺苷酰基转移酶（PPAT，E.C. 2.7.7.3）催化辅酶A（CoA）生物合成的倒数第二步反应，即将腺苷酰基从ATP转移至4'-磷酸泛酰巯基乙胺，形成脱磷酸辅酶A。我们获得了来自大肠杆菌的天然PPAT及其与底物复合物的立方晶体。这些晶体属于空间群I23或I213，晶胞参数a = 135.5 Å。在铜Kα旋转阳极发生器上，这些晶体的衍射分辨率优于1.8 Å。不对称单元可能包含两个分子，对应的堆积密度为2.9 ų Da⁻¹。
