Characterization of the Complex of a Trifluoromethyl-Substituted Shikimate-Based Bisubstrate Inhibitor and 5-Enolpyruvylshikimate-3-phosphate Synthase by REDOR NMR

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• 作者：Lynda M. McDowell ; Daniel R. Studelska ; Barbara Poliks ; R. D. O'Connor ; and Jacob Schaefer
• 刊名：Biochemistry
• 出版年：2004
• 出版时间：June 1, 2004
• 年：2004
• 卷：43
• 期：21
• 页码：6606 - 6611
• 全文大小：125K
• 年卷期：v.43,no.21(June 1, 2004)
• ISSN：1520-4995

文摘

A combination of ¹⁵N{¹⁹F}, ³¹P{¹⁵N}, and ³¹P{¹⁹F} rotational-echo double-resonance NMRhas been used to characterize the conformation of a bound trifluoromethylketal, shikimate-based bisubstrateinhibitor of 5-enolpyruvylshikimate-3-phosphate synthase. The solid-state NMR experiments wereperformed on the complex formed in solution and then lyophilized at low temperatures in the presence ofstabilizing lyoprotectants. The results of these experiments indicate that none of the side chains of the sixarginines that surround the active site forms a compact salt bridge with the phosphate groups of thebound inhibitor.