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

Van Horn WD, Kim HJ, Ellis CD, Hadziselimovic A, Sulistijo ES, Karra MD, Tian C, Sönnichsen FD, Sanders CR
Science. 2009 324 (5935): 1726-9

PMID: 19556511 · PMCID: PMC2764269 · DOI:10.1126/science.1171716

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.

MeSH Terms (17)

Adenosine Triphosphate Amino Acid Sequence Biocatalysis Catalytic Domain Cell Membrane Diacylglycerol Kinase Escherichia coli Escherichia coli Proteins Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary

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