4up6

Crystal structure of the wild-type diacylglycerol kinase refolded in the lipid cubic phase

spinqualitylabelsall models 4up6, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4up6 is a 3 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.801Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Diacylglycerol kinase 3D structures

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