7DVM
DgkA structure in E.coli lipid bilayer
Summary for 7DVM
| Entry DOI | 10.2210/pdb7dvm/pdb |
| Descriptor | Diacylglycerol kinase (1 entity in total) |
| Functional Keywords | enzyme, embedded in e.coli lipid bilayer, paramagnetic labelling, cs-rosetta, membrane protein |
| Biological source | Escherichia coli IAI39 |
| Total number of polymer chains | 3 |
| Total formula weight | 47580.49 |
| Authors | |
| Primary citation | Li, J.,Shen, Y.,Chen, Y.,Zhang, Z.,Ma, S.,Wan, Q.,Tong, Q.,Glaubitz, C.,Liu, M.,Yang, J. Structure of membrane diacylglycerol kinase in lipid bilayers. Commun Biol, 4:282-282, 2021 Cited by PubMed 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. PubMed: 33674677DOI: 10.1038/s42003-021-01802-1 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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