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Structure of membrane diacylglycerol kinase in lipid bilayers
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 crystallogr...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7935881/ https://www.ncbi.nlm.nih.gov/pubmed/33674677 http://dx.doi.org/10.1038/s42003-021-01802-1 |
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author | Li, Jianping Shen, Yang Chen, Yanke Zhang, Zhengfeng Ma, Shaojie Wan, Qianfen Tong, Qiong Glaubitz, Clemens Liu, Maili Yang, Jun |
author_facet | Li, Jianping Shen, Yang Chen, Yanke Zhang, Zhengfeng Ma, Shaojie Wan, Qianfen Tong, Qiong Glaubitz, Clemens Liu, Maili Yang, Jun |
author_sort | Li, Jianping |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7935881 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-79358812021-03-19 Structure of membrane diacylglycerol kinase in lipid bilayers Li, Jianping Shen, Yang Chen, Yanke Zhang, Zhengfeng Ma, Shaojie Wan, Qianfen Tong, Qiong Glaubitz, Clemens Liu, Maili Yang, Jun Commun Biol Article 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. Nature Publishing Group UK 2021-03-05 /pmc/articles/PMC7935881/ /pubmed/33674677 http://dx.doi.org/10.1038/s42003-021-01802-1 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Li, Jianping Shen, Yang Chen, Yanke Zhang, Zhengfeng Ma, Shaojie Wan, Qianfen Tong, Qiong Glaubitz, Clemens Liu, Maili Yang, Jun Structure of membrane diacylglycerol kinase in lipid bilayers |
title | Structure of membrane diacylglycerol kinase in lipid bilayers |
title_full | Structure of membrane diacylglycerol kinase in lipid bilayers |
title_fullStr | Structure of membrane diacylglycerol kinase in lipid bilayers |
title_full_unstemmed | Structure of membrane diacylglycerol kinase in lipid bilayers |
title_short | Structure of membrane diacylglycerol kinase in lipid bilayers |
title_sort | structure of membrane diacylglycerol kinase in lipid bilayers |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7935881/ https://www.ncbi.nlm.nih.gov/pubmed/33674677 http://dx.doi.org/10.1038/s42003-021-01802-1 |
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