7DVM

DgkA structure in E.coli lipid bilayer

7DVM の概要

• エントリーDOI: 10.2210/pdb7dvm/pdb
• 分子名称: Diacylglycerol kinase (1 entity in total)
• 機能のキーワード: enzyme, embedded in e.coli lipid bilayer, paramagnetic labelling, cs-rosetta, membrane protein
• 由来する生物種: Escherichia coli IAI39
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 47580.49

構造登録者

Li, J.,Yang, J. (登録日: 2021-01-13, 公開日: 2022-04-13, 最終更新日: 2023-09-27)

主引用文献

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

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: 33674677
DOI: 10.1038/s42003-021-01802-1

実験手法

SOLID-STATE NMR