6irc
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==C-terminal domain of Drosophila phospholipase b NORPA, methylated== | ==C-terminal domain of Drosophila phospholipase b NORPA, methylated== | ||
- | <StructureSection load='6irc' size='340' side='right' caption='[[6irc]], [[Resolution|resolution]] 3.54Å' scene=''> | + | <StructureSection load='6irc' size='340' side='right'caption='[[6irc]], [[Resolution|resolution]] 3.54Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6irc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRC OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6irc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IRC FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.538Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6irc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irc OCA], [https://pdbe.org/6irc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6irc RCSB], [https://www.ebi.ac.uk/pdbsum/6irc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6irc ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/PIPA_DROME 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]<ref>PMID:2457447</ref> <ref>PMID:25639794</ref> |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:30526850</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6irc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Drosophila melanogaster]] |
- | [[Category: Huang | + | [[Category: Large Structures]] |
- | [[Category: Li | + | [[Category: Huang Y]] |
- | [[Category: Liu | + | [[Category: Li J]] |
- | [[Category: Ye | + | [[Category: Liu W]] |
- | [[Category: Zhang | + | [[Category: Ye F]] |
- | + | [[Category: Zhang M]] | |
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Current revision
C-terminal domain of Drosophila phospholipase b NORPA, methylated
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Categories: Drosophila melanogaster | Large Structures | Huang Y | Li J | Liu W | Ye F | Zhang M