Description

Diacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues

Diacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues per subunit, means that available protein must be used economically to craft three catalytic and substrate-binding sites centred about the membrane/cytosol interface. How nature has accomplished this extraordinary feat is revealed here in a crystal structure of the kinase captured as a ternary complex with bound lipid substrate and an ATP analogue.

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    Date Created
    • 2015-12-17
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.1038/ncomms10140
    • Identifier Type
      International standard serial number
      Identifier Value
      2041-1723
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    Li, D., Stansfeld, P. J., Sansom, M. S., Keogh, A., Vogeley, L., Howe, N., . . . Caffrey, M. (2015). Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nature Communications, 6, 10140. doi:10.1038/ncomms10140

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