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| | <StructureSection load='4up6' size='340' side='right'caption='[[4up6]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='4up6' size='340' side='right'caption='[[4up6]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4up6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UP6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4up6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UP6 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diacylglycerol_kinase Diacylglycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.107 2.7.1.107] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.801Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4up6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4up6 OCA], [http://pdbe.org/4up6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4up6 RCSB], [http://www.ebi.ac.uk/pdbsum/4up6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4up6 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4up6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4up6 OCA], [https://pdbe.org/4up6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4up6 RCSB], [https://www.ebi.ac.uk/pdbsum/4up6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4up6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KDGL_ECOLI KDGL_ECOLI]] Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | + | [https://www.uniprot.org/uniprot/KDGL_ECOLI KDGL_ECOLI] Recycling of diacylglycerol produced during the turnover of membrane phospholipid. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Diacylglycerol kinase|Diacylglycerol kinase]] | + | *[[Diacylglycerol kinase 3D structures|Diacylglycerol kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diacylglycerol kinase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Caffrey, M]] | + | [[Category: Caffrey M]] |
| - | [[Category: Li, D]] | + | [[Category: Li D]] |
| - | [[Category: 8 mag]]
| + | |
| - | [[Category: In meso]]
| + | |
| - | [[Category: In vitro folding]]
| + | |
| - | [[Category: Lipid cubic phase]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Monoacylglycerol]]
| + | |
| - | [[Category: Refolding]]
| + | |
| - | [[Category: Renaturation]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
KDGL_ECOLI Recycling of diacylglycerol produced during the turnover of membrane phospholipid.
Publication Abstract from PubMed
Membrane proteins play vital roles in the life of the cell and are important therapeutic targets. Producing them in large quantities, pure and fully functional is a major challenge. Many promising projects end when intractable aggregates or precipitates form. Here we show how such unfolded aggregates can be solubilized and the solution mixed with lipid to spontaneously self-assemble a bicontinuous cubic mesophase into the bilayer of which the protein, in a confined, chaperonin-like environment, reconstitutes with 100% efficiency. The test protein, diacylglycerol kinase, reconstituted in the bilayer of the mesophase, was then crystallized in situ by the in meso or lipid cubic phase method providing an X-ray structure to a resolution of 2.55 A. This highly efficient, inexpensive, simple and rapid approach should find application wherever properly folded, membrane reconstituted and functional proteins are required where the starting material is a denatured aggregate.
Renaturing membrane proteins in the lipid cubic phase, a nanoporous membrane mimetic.,Li D, Caffrey M Sci Rep. 2014 Jul 24;4:5806. doi: 10.1038/srep05806. PMID:25055873[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li D, Caffrey M. Renaturing membrane proteins in the lipid cubic phase, a nanoporous membrane mimetic. Sci Rep. 2014 Jul 24;4:5806. doi: 10.1038/srep05806. PMID:25055873 doi:http://dx.doi.org/10.1038/srep05806
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