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Science 26 June 2009:
Vol. 324. no. 5935, pp. 1726 - 1729
DOI: 10.1126/science.1171716
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Reports

Solution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase

Wade D. Van Horn,1,* Hak-Jun Kim,1,2,* Charles D. Ellis,1 Arina Hadziselimovic,1 Endah S. Sulistijo,1 Murthy D. Karra,1 Changlin Tian,1,3 Frank D. Sönnichsen,4 Charles R. Sanders1,{dagger}

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.

1 Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
2 Korea Polar Research Institute, Incheon 406-840, Korea.
3 School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026, P. R. China.
4 Otto Diels Institute for Organic Chemistry, Christian Albrechts University of Kiel, D-24098 Kiel, Germany.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: chuck.sanders{at}vanderbilt.edu

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