Full metadata
Title
Ternary structure reveals mechanism of a membrane diacylglycerol kinase
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 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. Residues, identified as essential for activity by mutagenesis, decorate the active site and are rationalized by the ternary structure. The γ-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane. A catalytic mechanism for this unique enzyme is proposed. The active site architecture shows clear evidence of having arisen by convergent evolution.
Date Created
2015-12-17
Contributors
- Li, Dianfan (Author)
- Stansfeld, Phillip J. (Author)
- Sansom, Mark S. P. (Author)
- Keogh, Aaron (Author)
- Vogeley, Lutz (Author)
- Howe, Nicole (Author)
- Lyons, Joseph A. (Author)
- Aragao, David (Author)
- Fromme, Petra (Author)
- Fromme, Raimund (Author)
- Basu, Shibom (Author)
- Grotjohann, Ingo (Author)
- Kupitz, Christopher (Author)
- Rendek, Kimberley (Author)
- Weierstall, Uwe (Author)
- Zatsepin, Nadia (Author)
- Cherezov, Vadim (Author)
- Liu, Wei (Author)
- Bandaru, Sateesh (Author)
- English, Niall J. (Author)
- Gati, Cornelius (Author)
- Barty, Anton (Author)
- Yefanov, Oleksandr (Author)
- Chapman, Henry N. (Author)
- Diederichs, Kay (Author)
- Messerschmidt, Marc (Author)
- Boutet, Sebastien (Author)
- Williams, Garth J. (Author)
- Seibert, M. Marvin (Author)
- Caffrey, Martin (Author)
- College of Liberal Arts and Sciences (Contributor)
- School of Molecular Sciences (Contributor)
- Biodesign Institute (Contributor)
- Applied Structural Discovery (Contributor)
- Department of Physics (Contributor)
Resource Type
Extent
12 pages
Language
eng
Copyright Statement
In Copyright
Primary Member of
Identifier
Digital object identifier: 10.1038/ncomms10140
Identifier Type
International standard serial number
Identifier Value
2041-1723
Series
NATURE COMMUNICATIONS
Handle
https://hdl.handle.net/2286/R.I.44394
Preferred Citation
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
Level of coding
minimal
Cataloging Standards
Note
The final version of this article, as published in Nature Communications, can be viewed online at: https://www.nature.com/articles/ncomms10140
System Created
- 2017-06-05 05:20:50
System Modified
- 2021-08-16 02:23:30
- 3 years 2 months ago
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