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Science. 2009 Jun 26;324(5935):1726-9. doi: 10.1126/science.1171716.

Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase.

Author information

1
Department of Biochemistry and Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.

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.

PMID:
19556511
PMCID:
PMC2764269
DOI:
10.1126/science.1171716
[Indexed for MEDLINE]
Free PMC Article

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