Abstract
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 language | English (US) |
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Pages (from-to) | 1726-1729 |
Number of pages | 4 |
Journal | Science |
Volume | 324 |
Issue number | 5935 |
DOIs | |
State | Published - Jun 26 2009 |
Externally published | Yes |
ASJC Scopus subject areas
- General