来自大肠杆菌的磷酸果糖激酶-2四聚体形式的结晶及初步晶体学分析，核糖激酶家族的一员。
Crystallization and preliminary crystallographic analysis of the tetrameric form of phosphofructokinase-2 from Escherichia coli, a member of the ribokinase family.
作者信息
Cabrera Ricardo, Caniuguir Andrés, Ambrosio Andre L B, Guixé Victoria, Garratt Richard C, Babul Jorge
机构信息
Laboratorio de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Casilla 653, Santiago, Chile.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt 9):935-7. doi: 10.1107/S1744309106032246. Epub 2006 Aug 26.
Escherichia coli contains two phosphofructokinases, Pfk-1 and Pfk-2, which belong to unrelated protein families. In addition to catalytic function, the enzymes have converged in showing substrate inhibition by the nucleotide MgATP. However, although both Pfk-1 and Pfk-2 have been extensively characterized biochemically, only the structure of the former has been solved by X-ray diffraction. In order to fully understand how the same function has evolved on different structural folds, Pfk-2 has been crystallized by the hanging-drop vapour-diffusion method using PEG 6000 as precipitant. Single crystals were grown in the presence of MgATP and diffracted to 1.98 A. The crystals belong to the orthorhombic system, space group P222(1), with unit-cell parameters a = 42.8, b = 86.8, c = 171.3 A. The calculated Matthews coefficient of 2.45 A(3) Da(-1) indicates the presence of two monomers in the asymmetric unit, corresponding to a solvent content of 49%. Structure determination is ongoing.
大肠杆菌含有两种磷酸果糖激酶，即磷酸果糖激酶-1（Pfk-1）和磷酸果糖激酶-2（Pfk-2），它们属于不相关的蛋白质家族。除了催化功能外，这两种酶在受核苷酸MgATP的底物抑制方面表现出趋同现象。然而，尽管Pfk-1和Pfk-2都已在生化方面得到广泛表征，但只有前者的结构通过X射线衍射得以解析。为了全面了解相同功能是如何在不同的结构折叠上进化的，已使用PEG 6000作为沉淀剂，通过悬滴气相扩散法使Pfk-2结晶。在MgATP存在的情况下生长出单晶，并衍射至1.98 Å。这些晶体属于正交晶系，空间群为P222(1)，晶胞参数a = 42.8、b = 86.8、c = 171.3 Å。计算得到的马修斯系数为2.45 ų Da⁻¹，表明不对称单元中存在两个单体，对应溶剂含量为49%。结构解析工作正在进行中。
Zotero 插件