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Ternary structure reveals mechanism of a membrane diacylglycerol kinase

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Ternary structure reveals mechanism of a membrane diacylglycerol kinase. / Li, Dianfan; Stansfeld, Phillip J.; Sansom, Mark S P et al.
I: Nature Communications, Bind 6, 10140, 2015.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Li, D, Stansfeld, PJ, Sansom, MSP, Keogh, A, Vogeley, L, Howe, N, Lyons, JA, Aragao, D, Fromme, P, Fromme, R, Basu, S, Grotjohann, I, Kupitz, C, Rendek, K, Weierstall, U, Zatsepin, NA, Cherezov, V, Liu, W, Bandaru, S, English, NJ, Gati, C, Barty, A, Yefanov, O, Chapman, HN, Diederichs, K, Messerschmidt, M, Boutet, S, Williams, GJ, Seibert, MM & Caffrey, M 2015, 'Ternary structure reveals mechanism of a membrane diacylglycerol kinase', Nature Communications, bind 6, 10140. https://doi.org/10.1038/ncomms10140

APA

Li, D., Stansfeld, P. J., Sansom, M. S. P., Keogh, A., Vogeley, L., Howe, N., Lyons, J. A., Aragao, D., Fromme, P., Fromme, R., Basu, S., Grotjohann, I., Kupitz, C., Rendek, K., Weierstall, U., Zatsepin, N. A., Cherezov, V., Liu, W., Bandaru, S., ... Caffrey, M. (2015). Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nature Communications, 6, [10140]. https://doi.org/10.1038/ncomms10140

CBE

Li D, Stansfeld PJ, Sansom MSP, Keogh A, Vogeley L, Howe N, Lyons JA, Aragao D, Fromme P, Fromme R, et al. 2015. Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nature Communications. 6:Article 10140. https://doi.org/10.1038/ncomms10140

MLA

Li, Dianfan et al. "Ternary structure reveals mechanism of a membrane diacylglycerol kinase". Nature Communications. 2015. 6. https://doi.org/10.1038/ncomms10140

Vancouver

Li D, Stansfeld PJ, Sansom MSP, Keogh A, Vogeley L, Howe N et al. Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nature Communications. 2015;6:10140. doi: 10.1038/ncomms10140

Author

Li, Dianfan ; Stansfeld, Phillip J. ; Sansom, Mark S P et al. / Ternary structure reveals mechanism of a membrane diacylglycerol kinase. I: Nature Communications. 2015 ; Bind 6.

Bibtex

@article{d1220d0189a44532bdb166fdc58d7de2,
title = "Ternary structure reveals mechanism of a membrane diacylglycerol kinase",
abstract = "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 3-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.",
author = "Dianfan Li and Stansfeld, {Phillip J.} and Sansom, {Mark S P} and Aaron Keogh and Lutz Vogeley and Nicole Howe and Lyons, {Joseph A.} and David Aragao and Petra Fromme and Raimund Fromme and Shibom Basu and Ingo Grotjohann and Christopher Kupitz and Kimberley Rendek and Uwe Weierstall and Zatsepin, {Nadia A.} and Vadim Cherezov and Wei Liu and Sateesh Bandaru and English, {Niall J.} and Cornelius Gati and Anton Barty and Oleksandr Yefanov and Chapman, {Henry N.} and Kay Diederichs and Marc Messerschmidt and S{\'e}bastien Boutet and Williams, {Garth J.} and Seibert, {M. Marvin} and Martin Caffrey",
year = "2015",
doi = "10.1038/ncomms10140",
language = "English",
volume = "6",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Ternary structure reveals mechanism of a membrane diacylglycerol kinase

AU - Li, Dianfan

AU - Stansfeld, Phillip J.

AU - Sansom, Mark S P

AU - Keogh, Aaron

AU - Vogeley, Lutz

AU - Howe, Nicole

AU - Lyons, Joseph A.

AU - Aragao, David

AU - Fromme, Petra

AU - Fromme, Raimund

AU - Basu, Shibom

AU - Grotjohann, Ingo

AU - Kupitz, Christopher

AU - Rendek, Kimberley

AU - Weierstall, Uwe

AU - Zatsepin, Nadia A.

AU - Cherezov, Vadim

AU - Liu, Wei

AU - Bandaru, Sateesh

AU - English, Niall J.

AU - Gati, Cornelius

AU - Barty, Anton

AU - Yefanov, Oleksandr

AU - Chapman, Henry N.

AU - Diederichs, Kay

AU - Messerschmidt, Marc

AU - Boutet, Sébastien

AU - Williams, Garth J.

AU - Seibert, M. Marvin

AU - Caffrey, Martin

PY - 2015

Y1 - 2015

N2 - 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 3-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.

AB - 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 3-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.

UR - http://www.scopus.com/inward/record.url?scp=84950268487&partnerID=8YFLogxK

U2 - 10.1038/ncomms10140

DO - 10.1038/ncomms10140

M3 - Journal article

C2 - 26673816

AN - SCOPUS:84950268487

VL - 6

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 10140

ER -