Structure of membrane diacylglycerol kinase in lipid bilayers.
Structure of membrane diacylglycerol kinase in lipid bilayers.
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脂质双层膜二酰甘油激酶的结构
DOI：
10.1038/s42003-021-01802-1
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发表时间：
2021-03-05
影响因子：
5.9
通讯作者：
Yang J
中科院分区：
文献类型：
--
作者：
Li J;Shen Y;Chen Y;Zhang Z;Ma S;Wan Q;Tong Q;Glaubitz C;Liu M;Yang J
甘油二酯激酶（DgkA）是一种小的膜蛋白，负责ATP依赖性磷酸化甘油二酯为磷脂酸。它的结构在以前的研究中，确定在洗涤剂胶束溶液NMR和单油酸甘油酯立方相的X射线晶体学，显着不同。这些差异表明需要验证磷脂双层中这些基于洗涤剂的结构。在这里，我们提出了一个定义明确的同源三聚体结构的DgkA磷脂双层确定魔角旋转固态NMR（ssNMR）光谱，使用的方法结合内，分子间顺磁弛豫增强（PRE）衍生的距离限制和CS-Rosetta计算。在脂质双层中确定的DgkA结构不同于溶液NMR结构。此外，尽管DgkA的ssNMR结构显示出与X射线确定的结构类似的全局折叠，但这两种结构在单体对称性和动力学上不同。在三种不同的洗涤剂/脂质环境中确定的DgkA结构的比较分析提供了一个有意义的演示膜模拟环境的膜蛋白的结构和动力学的影响。Jianping Li等人提出了通过魔角旋转固态NMR光谱法测定的磷脂双层中的小整合膜蛋白二酰基甘油激酶（DgkA）的同源三聚体结构。他们将结构与溶液NMR和X射线晶体学解决的结构进行比较，并提供了对膜模拟环境对膜蛋白影响的见解。
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. Jianping Li et al. present the homo-trimeric structure of the small integral membrane protein diacylglycerol kinase (DgkA) in phospholipid bilayers determined by magic angle spinning solid-state NMR spectroscopy. They compare the structure with structures solved by solution NMR and X-ray crystallography and provide insights into the influence of membrane mimetic environments on membrane proteins.
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影响因子：
16.6
作者：
Li D;Stansfeld PJ;Sansom MSP;Keogh A;Vogeley L;Howe N;Lyons JA;Aragao D;Fromme P;Fromme R;Basu S;Grotjohann I;Kupitz C;Rendek K;Weierstall U;Zatsepin NA;Cherezov V;Liu W;Bandaru S;English NJ;Gati C;Barty A;Yefanov O;Chapman HN;Diederichs K;Messerschmidt M;Boutet S;Williams GJ;Marvin Seibert M;Caffrey M
通讯作者：
Caffrey M
影响因子：
1.7
作者：
Baldus, M;Petkova, AT;Griffin, RG
通讯作者：
Griffin, RG
影响因子：
2.9
作者：
Lau, FW;Chen, X;Bowie, JU
通讯作者：
Bowie, JU
影响因子：
14.8
作者：
通讯作者：
--
影响因子：
15
作者：
Linser, Rasmus;Fink, Uwe;Reif, Bernd
通讯作者：
Reif, Bernd