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1jad
From Proteopedia
(Difference between revisions)
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<StructureSection load='1jad' size='340' side='right'caption='[[1jad]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1jad' size='340' side='right'caption='[[1jad]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1jad]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1jad]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JAD 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]] 2.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | + | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jad OCA], [https://pdbe.org/1jad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jad RCSB], [https://www.ebi.ac.uk/pdbsum/1jad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jad ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jad OCA], [https://pdbe.org/1jad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jad RCSB], [https://www.ebi.ac.uk/pdbsum/1jad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jad ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q91086_MELGA Q91086_MELGA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jad ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jad ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | GTP-bound subunits of the Gq family of G alpha subunits directly activate phospholipase C-beta (PLC-beta) isozymes to produce the second messengers inositol 1,4,5-trisphosphate and diacylglycerol. PLC-betas are GTPase activating proteins (GAPs) that also promote the formation of GDP-bound, inactive G beta subunits. Both phospholipase activation by G alpha-GTP subunits and GAP activity require a C-terminal region unique to PLC-beta isozymes. The crystal structure of the C-terminal region from an avian PLC-beta, determined at 2.4 A resolution, reveals a novel fold composed almost entirely of three long helices forming a coiled-coil that dimerizes along its long axis in an antiparallel orientation. The dimer interface is extensive ( approximately 3,200 A(2)), and, based on gel exclusion chromatography, full length PLC-betas are dimeric, indicating that PLC-betas likely function as dimers. Sequence conservation, mutational data and molecular modeling show that an electrostatically positive surface of the dimer contains the major determinants for binding G beta q. Effector dimerization, as highlighted by PLC-betas, provides a viable mechanism for regulating signaling cascades linked to heterotrimeric G proteins. | ||
| - | |||
| - | A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q.,Singer AU, Waldo GL, Harden TK, Sondek J Nat Struct Biol. 2002 Jan;9(1):32-6. PMID:11753430<ref>PMID:11753430</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1jad" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Phospholipase C|Phospholipase C]] | *[[Phospholipase C|Phospholipase C]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Meleagris gallopavo]] |
| - | + | [[Category: Harden TK]] | |
| - | [[Category: Harden | + | [[Category: Singer AU]] |
| - | [[Category: Singer | + | [[Category: Sondek J]] |
| - | [[Category: Sondek | + | [[Category: Waldo GL]] |
| - | [[Category: Waldo | + | |
| - | + | ||
| - | + | ||
Current revision
C-terminal Domain of Turkey PLC-beta
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