Conformation and topology of diacylglycerol kinase in E.coli membranes revealed by solid-state NMR spectroscopy.
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.
Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071 (PR China).
Yanke
Y
Chen
Zhengfeng
Z
Zhang
Xinqi
X
Tang
Jianping
J
Li
Clemens
C
Glaubitz
Jun
J
Yang
D018360:Crystallography, X-Ray; D019852:Diacylglycerol Kinase / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
D019852:Diacylglycerol Kinase
diacylglycerol kinase; membrane proteins; protein structures; solid-state NMR; structure elucidation