3BQ7
SAM domain of Diacylglycerol Kinase delta1 (E35G)
Summary for 3BQ7
| Entry DOI | 10.2210/pdb3bq7/pdb |
| Descriptor | Diacylglycerol kinase delta (1 entity in total) |
| Functional Keywords | sam domain, polymerization domain, alternative splicing, cytoplasm, kinase, membrane, metal-binding, phorbol-ester binding, phosphoprotein, transferase, zinc, zinc-finger |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 2: Cytoplasm . Isoform 1: Membrane ; Peripheral membrane protein : Q16760 |
| Total number of polymer chains | 6 |
| Total formula weight | 57606.76 |
| Authors | Knight, M.J.,Bowie, J.U.,Sawaya, M.R. (deposition date: 2007-12-19, release date: 2008-03-25, Last modification date: 2023-08-30) |
| Primary citation | Harada, B.T.,Knight, M.J.,Imai, S.,Qiao, F.,Ramachander, R.,Sawaya, M.R.,Gingery, M.,Sakane, F.,Bowie, J.U. Regulation of Enzyme Localization by Polymerization: Polymer Formation by the SAM Domain of Diacylglycerol Kinase delta1 Structure, 16:380-387, 2008 Cited by PubMed Abstract: The diacylglycerol kinase (DGK) enzymes function as regulators of intracellular signaling by altering the levels of the second messengers, diacylglycerol and phosphatidic acid. The DGK delta and eta isozymes possess a common protein-protein interaction module known as a sterile alpha-motif (SAM) domain. In DGK delta, SAM domain self-association inhibits the translocation of DGK delta to the plasma membrane. Here we show that DGK delta SAM forms a polymer and map the polymeric interface by a genetic selection for soluble mutants. A crystal structure reveals that DGKSAM forms helical polymers through a head-to-tail interaction similar to other SAM domain polymers. Disrupting polymerization by polymer interface mutations constitutively localizes DGK delta to the plasma membrane. Thus, polymerization of DGK delta regulates the activity of the enzyme by sequestering DGK delta in an inactive cellular location. Regulation by dynamic polymerization is an emerging theme in signal transduction. PubMed: 18334213DOI: 10.1016/j.str.2007.12.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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