Brown Kathrin L, Morris Van K, Izard Tina
Department of Hematology-Oncology, St Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):195-6. doi: 10.1107/s0907444903025988. Epub 2003 Dec 18.
The penultimate step of prokaryotic coenzyme A (CoA) biosynthesis is directed by the essential enzyme phosphopantetheine adenylyltransferase (PPAT; EC 2.7.7.3), an attractive target for antibiotics. The reaction catalyzed by PPAT is rate-limiting and involves the transfer of an adenylyl group from ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA. Rhombohedral crystals of PPAT from Mycobacterium tuberculosis (Rv2965c) were obtained. The crystals belong to space group R32, with unit-cell parameters a = 68.69 A, alpha = 91.81 degrees. The crystals diffract to better than 2 A resolution on a Cu Kalpha rotating-anode generator. The packing density for one polypeptide chain in the asymmetric unit is 2.89 A(3) Da(-1), with a solvent content of 0.57.
原核生物辅酶A（CoA）生物合成的倒数第二步由必需酶磷酸泛酰巯基乙胺腺苷酰转移酶（PPAT；EC 2.7.7.3）指导，该酶是抗生素的一个有吸引力的靶点。PPAT催化的反应是限速反应，涉及将腺苷酰基从ATP转移到4'-磷酸泛酰巯基乙胺以形成3'-脱磷酸-CoA。获得了来自结核分枝杆菌（Rv2965c）的PPAT的菱形晶体。这些晶体属于空间群R32，晶胞参数a = 68.69 Å，α = 91.81°。在铜Kα旋转阳极发生器上，这些晶体的衍射分辨率优于2 Å。不对称单元中一条多肽链的堆积密度为2.89 ų Da⁻¹，溶剂含量为0.57。
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