Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid‐state NMR Spectroscopy1. (2nd April 2014)

• Record Type: Journal Article
• Authors: Chen, Yanke; Zhang, Zhengfeng; Tang, Xinqi; Li, Jianping; Glaubitz, Clemens; Yang, Jun
• Is Part Of: Angewandte Chemie. Volume 126:Number 22(2014)
• Page Start: 5730
• Page End: 5734
• Publication Date: 2014-04-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201311203
• Languages: English
• ISSNs: 0044-8249

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Solid‐state NMR is a powerful tool for studying membrane proteins in a native‐like lipid environment. 3D magic angle spinning (MAS) NMR was employed to characterize the structure of <italic>E.coli</italic> diacylglycerol kinase (DAGK) reconstituted into its native <italic>E.coli</italic> lipid membranes. The secondary structure and topology of DAGK revealed by solid‐state NMR are different from those determined by solution‐state NMR and X‐ray crystallography. This study provides a good example for demonstrating the influence of membrane environments on the structure of membrane proteins.</p> </abstract>