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New page: left|200px<br /><applet load="1jad" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jad, resolution 2.40Å" /> '''C-terminal Domain of...
 
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[[Image:1jad.gif|left|200px]]<br /><applet load="1jad" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jad, resolution 2.40&Aring;" />
'''C-terminal Domain of Turkey PLC-beta'''<br />


==Overview==
==C-terminal Domain of Turkey PLC-beta==
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.
<StructureSection load='1jad' size='340' side='right'caption='[[1jad]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q91086_MELGA Q91086_MELGA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/1jad_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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="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.


==About this Structure==
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>
1JAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JAD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11753430 11753430]
</div>
<div class="pdbe-citations 1jad" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Phospholipase C|Phospholipase C]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Harden TK]]
[[Category: Single protein]]
[[Category: Singer AU]]
[[Category: Harden, T.K.]]
[[Category: Sondek J]]
[[Category: Singer, A.U.]]
[[Category: Waldo GL]]
[[Category: Sondek, J.]]
[[Category: Waldo, G.L.]]
[[Category: SO4]]
[[Category: alpha helical coiled coil]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:21:30 2007''
Retrieved from "https://proteopedia.org/1jad"