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Solution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase

Science  26 Jun 2009:
Vol. 324, Issue 5935, pp. 1726-1729
DOI: 10.1126/science.1171716

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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.

  • * These authors contributed equally to this work.

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