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1jad

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[[Image:1jad.gif|left|200px]]
 
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{{Structure
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==C-terminal Domain of Turkey PLC-beta==
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|PDB= 1jad |SIZE=350|CAPTION= <scene name='initialview01'>1jad</scene>, resolution 2.40&Aring;
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<StructureSection load='1jad' size='340' side='right'caption='[[1jad]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<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>
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|ACTIVITY= <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>
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</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>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jad OCA], [http://www.ebi.ac.uk/pdbsum/1jad PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jad RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q91086_MELGA Q91086_MELGA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/1jad_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''C-terminal Domain of Turkey PLC-beta'''
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==See Also==
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*[[Phospholipase C|Phospholipase C]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1JAD is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/11753430 11753430]
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[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
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[[Category: Phosphoinositide phospholipase C]]
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[[Category: Harden TK]]
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[[Category: Single protein]]
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[[Category: Singer AU]]
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[[Category: Harden, T K.]]
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[[Category: Sondek J]]
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[[Category: Singer, A U.]]
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[[Category: Waldo GL]]
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[[Category: Sondek, J.]]
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[[Category: Waldo, G L.]]
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[[Category: alpha helical coiled coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:30:45 2008''
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Current revision

C-terminal Domain of Turkey PLC-beta

PDB ID 1jad

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