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Crystal structure of the integral membrane diacylglycerol kinase

Dianfan Li, Joseph A. Lyons, Valerie E. Pye, Lutz Vogeley, David Aragão, Colin P. Kenyon, Syed T. A. Shah, Christine Doherty, Margaret Aherne and Martin Caffrey ()
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Dianfan Li: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Joseph A. Lyons: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Valerie E. Pye: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Lutz Vogeley: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
David Aragão: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Colin P. Kenyon: CSIR, Biosciences, Meiring-Naude Road, Pretoria 0184, Gauteng, South Africa
Syed T. A. Shah: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Christine Doherty: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Margaret Aherne: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland
Martin Caffrey: School of Biochemistry and Immunology & School of Medicine, Trinity College Dublin, Dublin 2, Ireland

Nature, 2013, vol. 497, issue 7450, 521-524

Abstract: This study presents the crystal structures of three functional forms of diacylglycerol kinase, an integral membrane protein that catalyses a crucial step in oligosaccharide and lipopolysaccharide synthesis and assembly; these X-ray structures are markedly different from the only other structure available for this unique kinase that was solved using solution NMR.

Date: 2013
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DOI: 10.1038/nature12179

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