Diacylglycerol kinase

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== Structural highlights ==
== Structural highlights ==
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In DAGK DgkB the <scene name='70/706738/Cv/2'>nucleotide binding site</scene> is found at the interface between the 2 domains of the structure. <ref>PMID:18611377</ref>
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In DAGK DgkB the <scene name='70/706738/Cv/3'>nucleotide binding site</scene> is found at the interface between the 2 domains of the structure. <ref>PMID:18611377</ref> Water molrcules are shown asred spheres.
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</StructureSection>
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== 3D Structures of diacylglycerol kinase ==
== 3D Structures of diacylglycerol kinase ==
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[[Diacylglycerol kinase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Diacylglycerol kinase DgkA
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**[[3ze4]], [[4up6]], [[5d6i]], [[5dwk]] – EcDAGK – ''Escherichia coli'' <br />
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**[[2kdc]] – EcDAGK - NMR <br />
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**[[3ze3]], [[3ze5]], [[4bpd]], [[4brb]], [[4brr]], [[4d2e]], [[4cjz]], [[4ck0]], [[4uxw]], [[4uxz]], [[4uyo]], [[5d56]], [[5d57]] – EcDAGK (mutant) <br />
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**[[1tuz]] – hDAGK α – human<br />
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**[[3bq7]] – hDAGK δ1 SAM domain (mutant) <br />
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**[[1r79]] – hDAGK δ1 C1 domain - NMR<br />
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**[[3s40]] – DAGK – Bacillus anthracis<br />
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**[[4wer]] – DAGK catalytic domain – ''Enterococcus faecalis''<br />
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*Diacylglycerol kinase DgkB
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**[[2qvl]] – DgkB – ''Staphylococcus aureus''<br />
 
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**[[2qv7]] – DgkB + ADP<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Diacylglycerol kinase DkgB complex with ADP and Mg+2 ion (green) (PDB code 2qv7)

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References

  1. Merida I, Avila-Flores A, Merino E. Diacylglycerol kinases: at the hub of cell signalling. Biochem J. 2008 Jan 1;409(1):1-18. PMID:18062770 doi:http://dx.doi.org/10.1042/BJ20071040
  2. Miller DJ, Jerga A, Rock CO, White SW. Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases. Structure. 2008 Jul;16(7):1036-46. PMID:18611377 doi:http://dx.doi.org/10.1016/j.str.2008.03.019

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