Ternary structure reveals mechanism of a membrane diacylglycerol kinase-Reference-Cited by-同舟云学术

Ternary structure reveals mechanism of a membrane diacylglycerol kinase

Published:2015-12 Issue:1 Volume:6 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Li Dianfan,Stansfeld Phillip J.,Sansom Mark S. P.,Keogh Aaron,Vogeley Lutz,Howe Nicole,Lyons Joseph A.,Aragao David,Fromme Petra,Fromme Raimund,Basu Shibom,Grotjohann Ingo,Kupitz Christopher,Rendek Kimberley,Weierstall Uwe,Zatsepin Nadia A.,Cherezov Vadim,Liu Wei,Bandaru Sateesh,English Niall J.,Gati Cornelius,Barty Anton,Yefanov Oleksandr,Chapman Henry N.,Diederichs Kay,Messerschmidt Marc,Boutet Sébastien,Williams Garth J.,Marvin Seibert M.,Caffrey Martin

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms10140.pdf

Reference48 articles.

1. Van Horn, W. D. & Sanders, C. R. Prokaryotic diacylglycerol kinase and undecaprenol kinase. Annu. Rev. Biophys. 41, 81–101 (2012).

2. Badola, P. & Sanders, C. R. Escherichia coli diacylglycerol kinase is an evolutionarily optimized membrane enzyme and catalyzes direct phosphoryl transfer. J. Biol. Chem. 272, 24176–24182 (1997).

3. Lau, F. W., Chen, X. & Bowie, J. U. Active sites of diacylglycerol kinase from Escherichia coli are shared between subunits. Biochemistry 38, 5521–5527 (1999).

4. Mi, D., Kim, H. J., Hadziselimovic, A. & Sanders, C. R. Irreversible misfolding of diacylglycerol kinase is independent of aggregation and occurs prior to trimerization and membrane association. Biochemistry 45, 10072–10084 (2006).

5. Sanders, C. R. et al. Escherichia coli diacylglycerol kinase is an alpha-helical polytopic membrane protein and can spontaneously insert into preformed lipid vesicles. Biochemistry 35, 8610–8618 (1996).

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