3BQ7

SAM domain of Diacylglycerol Kinase delta1 (E35G)

3BQ7 の概要

• エントリーDOI: 10.2210/pdb3bq7/pdb
• 分子名称: Diacylglycerol kinase delta (1 entity in total)
• 機能のキーワード: sam domain, polymerization domain, alternative splicing, cytoplasm, kinase, membrane, metal-binding, phorbol-ester binding, phosphoprotein, transferase, zinc, zinc-finger
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 2: Cytoplasm . Isoform 1: Membrane ; Peripheral membrane protein : Q16760
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 57606.76

構造登録者

Knight, M.J.,Bowie, J.U.,Sawaya, M.R. (登録日: 2007-12-19, 公開日: 2008-03-25, 最終更新日: 2023-08-30)

主引用文献

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

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: 18334213
DOI: 10.1016/j.str.2007.12.017

実験手法

X-RAY DIFFRACTION (2.9 Å)