Domain Activity Based Protein Structure Study of T-protein from Escherichia coli
基于结构域活性分析的大肠杆菌T蛋白结构研究

T-protein from Escherichia coli consists of three domains:chorismate mutase,prephenate dehydrogenase and a regulatory domain.In this study,the domain activity of several fragments from T-protein was evaluated.It was found that chorismate mutase domains' retained less activity,but was more stable,prephenate dehydrogenase domain retained more activity,but less stability.It lost all prephenate dehydrogenase activity when T-protein was expressed with 38 amino acids cut off at its C-terminus,but chorismate mutase and regulatory activity were both retained.It was concluded that chorismate mutase domain had an independent and compact structure,but prephenate dehydrogenase domain had a loose conformation interlaced with its regulatory domain.