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6irc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==C-terminal domain of Drosophila phospholipase b NORPA, methylated== | |
| + | <StructureSection load='6irc' size='340' side='right'caption='[[6irc]], [[Resolution|resolution]] 3.54Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6irc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6IRC FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">norpA, PLC-beta, CG3620 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6irc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6irc OCA], [http://pdbe.org/6irc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6irc RCSB], [http://www.ebi.ac.uk/pdbsum/6irc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6irc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6irc" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drome]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phosphoinositide phospholipase C]] | ||
| + | [[Category: Huang, Y]] | ||
| + | [[Category: Li, J]] | ||
[[Category: Liu, W]] | [[Category: Liu, W]] | ||
[[Category: Ye, F]] | [[Category: Ye, F]] | ||
| - | [[Category: | + | [[Category: Zhang, M]] |
| - | [[Category: | + | [[Category: Coiled coil]] |
| + | [[Category: Drosophila]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Phospholipase beta]] | ||
Current revision
C-terminal domain of Drosophila phospholipase b NORPA, methylated
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