Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Kristin Möbius, Sina Kazemi, Peter Güntert, Andreas Jakob, Alexander Heckel, Johanna Becker-Baldus, Clemens Glaubitz

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. More... »

PAGES

3995

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-019-40264-8

DOI

http://dx.doi.org/10.1038/s41598-019-40264-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112641500

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30850624


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