%0 Journal Article
%T Domain Activity Based Protein Structure Study of T-protein from Escherichia coli<br>基于结构域活性分析的大肠杆菌T蛋白结构研究
%A YING Yue-bin
%A SONG Jian-hui
%A HUANG Peng
%A CHEN Shu-qing
%A <br>应跃斌
%A 宋见惠
%A 黄鹏
%A 陈枢青
%J 生物物理学报
%D 2006
%I 
%X 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.
%K Escherichia coli
%K T-protein
%K Chorismate mutase
%K Prephenate dehydrogenase
%K Regulatory domain<br>大肠杆菌
%K T蛋白
%K 分支酸变位酶
%K 预苯酸脱氢酶
%K 调节结构域
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=B8D3909B19B9FC67&yid=37904DC365DD7266&vid=BC12EA701C895178&iid=94C357A881DFC066&sid=302684F6FB4B24FF&eid=A04F01817ECB9A48&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=0&reference_num=10