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周丛照
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期刊论文
Activation of the LicT Transcriptional Antiterminator Involves a Domain Swing⁄Lock Mechanism Provoking Massive Structural Changes*□
THE JOURNAL OF BIOLOGICAL CHEMISTRY 280(15)14780-14789, 2005，-0001，（）：
The transcriptional antiterminator protein Lic Tregulates the expression of Bacillus subtilis operons involved in-glucoside metabolism. It consists of an Nterminal RNA-binding domain (co-antiterminator (CAT)) and two phosphorylatable phosphotransferase system regulation domains (PRD1 and PRD2). In the activated state, each PRD forms a dimericunit with the phosphorylation sites totally buried at the dimer interface. Here we present the 1.95
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