ArticleScientific reports2019
Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Mechanistic Insight into the Mechanical Unfolding of the Integral Membrane Diacylglycerol Kinase.JACS Au · 2024Article
- Structural and functional consequences of the H180A mutation of the light-driven sodium pump KR2.Biophysical journal · 2023Article
- Applications of Cell-Free Synthesized Membrane Protein Precipitates.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structure of membrane diacylglycerol kinase in lipid bilayers.Communications biology · 2021Article
- Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-RangeThe journal of physical chemistry. B · 2020Article
- Light-Induced Uncaging for Time-Resolved Observations of Biochemical Reactions by MAS NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
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Authors and funding
7 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli diacylglycerol kinase (DGK) is an integral membrane protein, which catalyses the ATP-dependent phosphorylation of diacylglycerol (DAG) to phosphatic acid (PA). It is a unique trimeric enzyme, which does not share sequence homology with typical kinases. It exhibits a notable complexity in structure and function despite of its small size. Here, chemical shift assignment of wild-type DGK within lipid bilayers was carried out based on 3D MAS NMR, utilizing manual and automatic analysis protocols. Upon nucleotide binding, extensive chemical shift perturbations could be observed. These data provide evidence for a symmetric DGK trimer with all of its three active sites concurrently occupied. Additionally, we could detect that the nucleotide substrate induces a substantial conformational change, most likely directing DGK into its catalytic active form. Furthermore, functionally relevant interprotomer interactions are identified by DNP-enhanced MAS NMR in combination with site-directed mutagenesis and functional assays.
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