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Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid‐state NMR Spectroscopy
Author(s) -
Chen Yanke,
Zhang Zhengfeng,
Tang Xinqi,
Li Jianping,
Glaubitz Clemens,
Yang Jun
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201311203
Subject(s) - diacylglycerol kinase , membrane , solid state nuclear magnetic resonance , magic angle spinning , nuclear magnetic resonance spectroscopy , chemistry , membrane topology , topology (electrical circuits) , membrane protein , crystallography , biophysics , stereochemistry , biochemistry , kinase , protein kinase c , biology , nuclear magnetic resonance , physics , mathematics , combinatorics
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 E.coli diacylglycerol kinase (DAGK) reconstituted into its native E.coli 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.