Structure of membrane diacylglycerol kinase in lipid bilayers. 2021

Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
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.

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.

UI MeSH Term Description Entries
D008051 Lipid Bilayers Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes. Bilayers, Lipid,Bilayer, Lipid,Lipid Bilayer
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D010743 Phospholipids Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system. Phosphatides,Phospholipid
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003902 Detergents Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties. Cleansing Agents,Detergent Pods,Laundry Detergent Pods,Laundry Pods,Syndet,Synthetic Detergent,Agent, Cleansing,Agents, Cleansing,Cleansing Agent,Detergent,Detergent Pod,Detergent Pod, Laundry,Detergent Pods, Laundry,Detergent, Synthetic,Detergents, Synthetic,Laundry Detergent Pod,Laundry Pod,Pod, Detergent,Pod, Laundry,Pod, Laundry Detergent,Pods, Detergent,Pods, Laundry,Pods, Laundry Detergent,Synthetic Detergents
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D017510 Protein Folding Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D055503 Protein Multimerization The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS. Protein Dimerization,Protein Heteromultimerizaton,Protein Multimer Assembly,Protein Trimerization,Assembly, Protein Multimer,Dimerization, Protein,Heteromultimerizaton, Protein,Heteromultimerizatons, Protein,Multimer Assembly, Protein,Multimerization, Protein,Trimerization, Protein
D019852 Diacylglycerol Kinase An enzyme of the transferase class that uses ATP to catalyze the phosphorylation of diacylglycerol to a phosphatidate. EC 2.7.1.107. DAG Kinase,Diacylglycerol Kinase alpha (DGKA),Diglyceride Kinase,1,2-Diacylglycerol Kinase,Arachidonoyl-Diacylglycerol Kinase,Ceramide-Diglyceride Kinase,DGK alpha,DGK beta,DGK delta,DGK gamma,DGK-IV,DGKdelta,1,2 Diacylglycerol Kinase,Arachidonoyl Diacylglycerol Kinase,Ceramide Diglyceride Kinase,Kinase, 1,2-Diacylglycerol,Kinase, Arachidonoyl-Diacylglycerol,Kinase, Ceramide-Diglyceride,Kinase, DAG,Kinase, Diacylglycerol,Kinase, Diglyceride,alpha, DGK,beta, DGK,delta, DGK,gamma, DGK

Related Publications

Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
May 2013, Nature,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
December 2017, Nature communications,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
December 2015, Nature communications,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
June 2009, Science (New York, N.Y.),
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
November 2000, Biochimica et biophysica acta,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
September 1984, The Journal of biological chemistry,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
December 2012, Biochimica et biophysica acta,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
November 2018, Analytical chemistry,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
March 1971, Nature: New biology,
Jianping Li, and Yang Shen, and Yanke Chen, and Zhengfeng Zhang, and Shaojie Ma, and Qianfen Wan, and Qiong Tong, and Clemens Glaubitz, and Maili Liu, and Jun Yang
September 1978, Biophysical journal,
Copied contents to your clipboard!