6irb | pdb_00006irb

C-terminal coiled coil domain of Drosophila phospholipase C beta NORPA, selenomethionine

spinqualitylabelsall models 6irb, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6irb is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: norpA, PLC-beta, CG3620 (DROME) Activity: Phosphoinositide phospholipase C, with EC number 3.1.4.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PIPA_DROME] The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (By similarity). Essential component of the phototransduction pathway (PubMed:2457447). Essential downstream component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required for the activation of Cad99C and consequently Cad99C-dependent endosome formation, which is essential for the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection (PubMed:25639794).[UniProtKB:Q9P212] Publication Abstract from PubMed INAD assembles key enzymes of the Drosophila 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 Cbeta, PLCbeta), 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 PLCbeta4 with a mode that is strikingly similar to that of the INAD-NORPA complex, as revealed by the structure of the INADL PDZ89-PLCbeta4 CC-PBM complex. Therefore, our study suggests that the highly specific PDZ tandem - PLCbeta interactions are an evolutionarily conserved mechanism in PLCbeta signaling in the animal kingdom. An unexpected INAD PDZ tandem-mediated plcbeta binding in Drosophila photo receptors.,Ye F, Huang Y, Li J, Ma Y, Xie C, Liu Z, Deng X, Wan J, Xue T, Liu W, Zhang M Elife. 2018 Dec 10;7. pii: 41848. doi: 10.7554/eLife.41848. PMID:30526850 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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