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- W169092238 abstract "E. coli diacylglycerol kinase (DAGK) is a trimeric 40 kDa a-helical integral membrane protein comprised of 9 transmembrane (TM) helices, which is important in phosphatidic acid metabolism. In this work, we present the 3D structure and corresponding structure-function data which detail the active site of the protein. We determined the structure of DAGK, which was folded in detergent micelles using NMR. We were able to generate an ensemble of DAGK structures with an RMSD of less than 1Å. The resulting structure represents a unique fold that has a threefold symmetry axis made of the 2nd TM of each monomer, forming a three helix bundle core. DAGK has an intricate fold with helices from different monomer subunits contributing to each of the three active sites. To map the active site, DAGK was titrated with substrates and followed by NMR. These data are in agreement with biochemical data which were generated by examining the effects of cysteine mutations on protein activity. Our results provide a platform for future studies of the folding and enzymatic mechanism of DAGK and illustrate the utility of NMR to investigate challenging membrane protein targets. Supported by NIH RO1GM47485." @default.
- W169092238 created "2016-06-24" @default.
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- W169092238 date "2009-04-01" @default.
- W169092238 modified "2023-09-27" @default.
- W169092238 title "NMR based structure and enzymatic insight into diacylglycerol kinase, an alpha‐helical membrane protein" @default.
- W169092238 doi "https://doi.org/10.1096/fasebj.23.1_supplement.lb223" @default.
- W169092238 hasPublicationYear "2009" @default.
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