Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase

Wade D. Van Horn, Hak Jun Kim, Charles D. Ellis, Arina Hadziselimovic, Endah S. Sulistijo, Murthy D. Karra, Changlin Tian, Frank D. Sönnichsen, Charles R. Sanders

Research output: Contribution to journalArticlepeer-review

182 Scopus citations


Escherichia coli diacylglycerol kinase (DAGK) represents a family of integral membrane enzymes that is unrelated to all other phosphotransferases. We have determined the three-dimensional structure of the DAGK homotrimer with the use of solution nuclear magnetic resonance. The third transmembrane helix from each subunit is domain-swapped with the first and second transmembrane segments from an adjacent subunit. Each of DAGK's three active sites resembles a portico. The cornice of the portico appears to be the determinant of DAGK's lipid substrate specificity and overhangs the site of phosphoryl transfer near the water-membrane interface. Mutations to cysteine that caused severe misfolding were located in or near the active site, indicating a high degree of overlap between sites responsible for folding and for catalysis.

Original languageEnglish (US)
Pages (from-to)1726-1729
Number of pages4
Issue number5935
StatePublished - Jun 26 2009
Externally publishedYes

ASJC Scopus subject areas

  • General


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