6IRC

C-terminal domain of Drosophila phospholipase b NORPA, methylated

Summary for 6IRC

• Entry DOI: 10.2210/pdb6irc/pdb
• Descriptor: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase (1 entity in total)
• Functional Keywords: phospholipase beta, coiled coil, drosophila, hydrolase
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 27533.68

Authors

Ye, F.,Li, J.,Huang, Y.,Liu, W.,Zhang, M. (deposition date: 2018-11-12, release date: 2019-01-02, Last modification date: 2020-10-28)

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

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: 30526850
DOI: 10.7554/eLife.41848

Experimental method

X-RAY DIFFRACTION (3.538 Å)