6IRB
C-terminal coiled coil domain of Drosophila phospholipase C beta NORPA, selenomethionine
Summary for 6IRB
Entry DOI | 10.2210/pdb6irb/pdb |
Descriptor | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase (2 entities in total) |
Functional Keywords | phospholipase c beta, coiled coil, drosophila selenomethionine, hydrolase |
Biological source | Drosophila melanogaster (Fruit fly) |
Total number of polymer chains | 2 |
Total formula weight | 50181.23 |
Authors | |
Primary citation | Ye, F.,Huang, Y.,Li, J.,Ma, Y.,Xie, C.,Liu, Z.,Deng, X.,Wan, J.,Xue, T.,Liu, W.,Zhang, M. An unexpected INAD PDZ tandem-mediated plc beta binding in Drosophila photo receptors. Elife, 7:-, 2018 Cited by PubMed Abstract: INAD assembles key enzymes of the compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. However, the molecular mechanism that governs the interaction between INAD and NORPA (phospholipase Cβ, PLCβ), a key step for the fast kinetics of the light signaling, is not known. Here, we show that the NORPA C-terminal coiled-coil domain and PDZ-binding motif (CC-PBM) synergistically bind to INAD PDZ45 tandem with an unexpected mode and unprecedented high affinity. Guided by the structure of the INAD-NORPA complex, we discover that INADL is probably a mammalian counterpart of INAD. The INADL PDZ89 tandem specifically binds to PLCβ4 with a mode that is strikingly similar to that of the INAD-NORPA complex, as revealed by the structure of the INADL PDZ89-PLCβ4 CC-PBM complex. Therefore, our study suggests that the highly specific PDZ tandem - PLCβ interactions are an evolutionarily conserved mechanism in PLCβ signaling in the animal kingdom. PubMed: 30526850DOI: 10.7554/eLife.41848 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.661 Å) |
Structure validation
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