Structure of membrane diacylglycerol kinase in lipid bilayers.

Commun Biol

National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, People's Republic of China.

Published: March 2021

AI Article Synopsis

  • Diacylglycerol kinase (DgkA) is an essential membrane protein that converts diacylglycerol to phosphatidic acid using ATP, with previous studies showing different structures depending on the environment used for analysis.
  • This research presents a detailed structure of DgkA in phospholipid bilayers obtained through advanced solid-state NMR techniques, highlighting significant differences from earlier solution NMR and X-ray crystallography findings.
  • The study underscores how varying detergent and lipid environments can affect the structure and dynamics of membrane proteins, demonstrating the importance of validating protein structures in more physiologically relevant settings.

Article Abstract

Diacylglycerol kinase (DgkA) is a small integral membrane protein, responsible for the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid. Its structures reported in previous studies, determined in detergent micelles by solution NMR and in monoolein cubic phase by X-ray crystallography, differ significantly. These differences point to the need to validate these detergent-based structures in phospholipid bilayers. Here, we present a well-defined homo-trimeric structure of DgkA in phospholipid bilayers determined by magic angle spinning solid-state NMR (ssNMR) spectroscopy, using an approach combining intra-, inter-molecular paramagnetic relaxation enhancement (PRE)-derived distance restraints and CS-Rosetta calculations. The DgkA structure determined in lipid bilayers is different from the solution NMR structure. In addition, although ssNMR structure of DgkA shows a global folding similar to that determined by X-ray, these two structures differ in monomeric symmetry and dynamics. A comparative analysis of DgkA structures determined in three different detergent/lipid environments provides a meaningful demonstration of the influence of membrane mimetic environments on the structure and dynamics of membrane proteins.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7935881PMC
http://dx.doi.org/10.1038/s42003-021-01802-1DOI Listing

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