Evidence map›Paper›PMID 26673816›Full record

ArticleNature communications2015

Ternary structure reveals mechanism of a membrane diacylglycerol kinase.

Dianfan Li, Phillip J Stansfeld, Mark S P Sansom, Aaron Keogh, Lutz Vogeley, Nicole Howe, Joseph A Lyons, David Aragao, Petra Fromme, Raimund Fromme and 20 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Serial femtosecond crystallography.Nature reviews. Methods primers · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Diacylglycerol kinases: Relationship to other lipid kinases.Advances in biological regulation · 2019
    Review
  13. Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018
    Review
  14. Article
  15. Article
  16. Structural basis for catalysis at the membrane-water interface.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

30 authors at 10 institutions in 4 countries.

Dianfan LiSchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Aaron KeoghSchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Lutz VogeleySchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Nicole HoweSchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Joseph A LyonsSchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
David AragaoSchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Petra FrommeSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Raimund FrommeSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Shibom BasuSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Ingo GrotjohannSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Christopher KupitzSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Kimberley RendekSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Uwe WeierstallDepartment of Physics, Arizona State University, Tempe, Arizona 85287, USA.
Nadia A ZatsepinDepartment of Physics, Arizona State University, Tempe, Arizona 85287, USA.
Vadim CherezovDepartment of Chemistry, Bridge Institute, University of Southern California, Los Angeles, California 90089, USA.
Wei LiuSchool of Molecular Sciences and Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona 85287, USA.
Sateesh BandaruSFI Strategic Research Cluster in Solar Energy Conversion, School of Chemical and Bioprocess Engineering, University College Dublin, Belfield, Dublin 4, Ireland.
Niall J EnglishSFI Strategic Research Cluster in Solar Energy Conversion, School of Chemical and Bioprocess Engineering, University College Dublin, Belfield, Dublin 4, Ireland.
Cornelius GatiCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron, 22607 Hamburg, Germany.
Anton BartyCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron, 22607 Hamburg, Germany.
Oleksandr YefanovCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron, 22607 Hamburg, Germany.
Henry N ChapmanCenter for Free Electron Laser Science, Deutsches Elektronen-Synchrotron, 22607 Hamburg, Germany.
Kay DiederichsDepartment of Biology, University of Konstanz, Box 647, D-78457 Konstanz, Germany.
Marc MesserschmidtLinac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA.
Sébastien BoutetLinac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA.
Garth J WilliamsLinac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA.
M Marvin SeibertLinac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA.
Martin CaffreySchool of Medicine and School of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Arizona State University · USTrinity College Dublin · IEUniversität Hamburg · DELinac Coherent Light Source · USSLAC National Accelerator Laboratory · USUniversity College Dublin · IEUniversity of Oxford · GBCenter for Free-Electron Laser Science · DEUniversity of Konstanz · DEUniversity of Southern California · US

Funding

Yeast ExpressionP50GM073210 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2004 to 2013
$21.5M
Center for the Rational Design of Membrane Protein CrystallographyU54GM094599 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2014
$6.8M
Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
HT structure determination of GPCRs by LCP serial femtosecond nanocrystallographyR01GM108635 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEREZOV, VADIM · 2014 to 2017
$1.5M
Membrane Proteins. Crystallogenesis/X-ray Structure(RMI)R01GM075915 · NIGMS · UNIVERSITY OF LIMERICK · PI CAFFREY, MARTIN D. · 2005 to 2009
$984k
Biotechnology and Biological Sciences Research Council BB/I019855/1Biotechnology and Biological Sciences Research Council BB/L002558/1NIGMS NIH HHS P50 GM073210NIGMS NIH HHS R01 GM075915NIGMS NIH HHS R01 GM095583NIGMS NIH HHS R01 GM108635NIGMS NIH HHS U54 GM094599Wellcome Trust
6 · The paper itself

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 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.

Indexed as

Adenosine TriphosphateBinding SitesCatalytic DomainCell MembraneCrystallography, X-RayDiacylglycerol KinaseEscherichia coliModels, MolecularProtein ConformationAdenosine TriphosphateDiacylglycerol Kinase

Identifiers

PMID26673816
PMCPMC4703834
OpenAlexW2272187853

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.