4brb: Difference between revisions
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<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=4brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4brb RCSB], [http://www.ebi.ac.uk/pdbsum/4brb PDBsum]</span></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=4brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4brb RCSB], [http://www.ebi.ac.uk/pdbsum/4brb PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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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</StructureSection> | </StructureSection> | ||
[[Category: Diacylglycerol kinase]] | [[Category: Diacylglycerol kinase]] | ||
[[Category: Caffrey, M | [[Category: Caffrey, M]] | ||
[[Category: Li, D | [[Category: Li, D]] | ||
[[Category: Lipid metabolism]] | [[Category: Lipid metabolism]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 02:11, 25 December 2014
Crystal structure of the integral membrane enzyme DgkA-ref, delta 7Crystal structure of the integral membrane enzyme DgkA-ref, delta 7
Structural highlights
Function[KDGL_ECOLI] Recycling of diacylglycerol produced during the turnover of membrane phospholipid. Publication Abstract from PubMedMembrane 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. References
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