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Three-dimensional structure of phosphoribosyl pyrophosphate synthetase from E-coli at 2.71 angstrom resolution

机译:大肠杆菌中2.71埃分辨率的磷酸核糖焦磷酸合成酶的三维结构

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Phosphoribosyl pyrophosphate synthetase from Escherichia coli was cloned, purified, and crystallized. Single crystals of the enzyme were grown under microgravity. The X-ray diffraction data set was collected at the Spring-8 synchrotron facility and used to determine the three-dimensional structure of the enzyme by the molecular-replacement method at 2.71 resolution. The active and regulatory sites in the molecule of E. coli phosphoribosyl pyrophosphate synthetase were revealed by comparison with the homologous protein from Bacillus subtilis, the structure of which was determined in a complex with functional ligands. The conformations of polypeptide-chain fragments surrounding and composing the active and regulatory sites were shown to be identical in both proteins.
机译:克隆,纯化和结晶了来自大肠杆菌的磷酸核糖焦磷酸合成酶。酶的单晶在微重力下生长。 X射线衍射数据集是在Spring-8同步加速器设施中收集的,用于通过分子置换方法以2.71分辨率确定酶的三维结构。通过与枯草芽孢杆菌的同源蛋白进行比较,揭示了大肠杆菌磷酸核糖焦磷酸合成酶分子中的活性和调控位点,该蛋白的结构是在具有功能性配体的复合物中确定的。在两种蛋白质中,围绕并组成活性和调节位点的多肽链片段的构象均显示为相同。

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