OCA at 08:06, 6 December 2023

OCA — Wed, 06 Dec 2023 08:06:34 GMT

←Older revision		Revision as of 08:06, 6 December 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8uqo is ~~ON HOLD until Paper~~ Publication	+	==PLCb3-Gbg-Gaq complex on membranes==
		+	<StructureSection load='8uqo' size='340' side='right'caption='[[8uqo]], [[Resolution\|resolution]] 3.37Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8uqo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UQO FirstGlance]. <br>
		+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.37Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8uqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8uqo OCA], [https://pdbe.org/8uqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8uqo RCSB], [https://www.ebi.ac.uk/pdbsum/8uqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8uqo ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/GBB1_HUMAN GBB1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.<ref>PMID:18611381</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	PLCbeta (Phospholipase Cbeta) enzymes cleave phosphatidylinositol 4,5-bisphosphate (PIP2) producing IP3 and DAG (diacylglycerol). PIP2 modulates the function of many ion channels, while IP3 and DAG regulate intracellular Ca(2+) levels and protein phosphorylation by protein kinase C, respectively. PLCbeta enzymes are under the control of G protein coupled receptor signaling through direct interactions with G proteins Gbetagamma and Galpha(q) and have been shown to be coincidence detectors for dual stimulation of Galpha(q) and Galpha(i)-coupled receptors. PLCbetas are aqueous-soluble cytoplasmic enzymes but partition onto the membrane surface to access their lipid substrate, complicating their functional and structural characterization. Using newly developed methods, we recently showed that Gbetagamma activates PLCbeta3 by recruiting it to the membrane. Using these same methods, here we show that Galpha(q) increases the catalytic rate constant, k(cat), of PLCbeta3. Since stimulation of PLCbeta3 by Galpha(q) depends on an autoinhibitory element (the X-Y linker), we propose that Galpha(q) produces partial relief of the X-Y linker autoinhibition through an allosteric mechanism. We also determined membrane-bound structures of the PLCbeta3.Galpha(q) and PLCbeta3.Gbetagamma(2).Galpha(q) complexes, which show that these G proteins can bind simultaneously and independently of each other to regulate PLCbeta3 activity. The structures rationalize a finding in the enzyme assay, that costimulation by both G proteins follows a product rule of each independent stimulus. We conclude that baseline activity of PLCbeta3 is strongly suppressed, but the effect of G proteins, especially acting together, provides a robust stimulus upon G protein stimulation.

-	~~Authors~~:	+	The mechanism of Galpha(q) regulation of PLCbeta3-catalyzed PIP2 hydrolysis.,Falzone ME, MacKinnon R Proc Natl Acad Sci U S A. 2023 Nov 28;120(48):e2315011120. doi: , 10.1073/pnas.2315011120. Epub 2023 Nov 22. PMID:37991948<ref>PMID:37991948</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8uqo" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Falzone ME]]
		+	[[Category: MacKinnon R]]

OCA at 09:09, 8 November 2023

OCA — Wed, 08 Nov 2023 09:09:58 GMT

←Older revision		Revision as of 09:09, 8 November 2023
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8uqo is ON HOLD	+	The entry 8uqo is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8uqo" [edit=sysop:move=sysop]

OCA — Wed, 01 Nov 2023 11:04:15 GMT

Protected "8uqo" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:04, 1 November 2023

OCA: New page: '''Unreleased structure''' The entry 8uqo is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 01 Nov 2023 11:04:13 GMT

New page: '''Unreleased structure''' The entry 8uqo is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8uqo is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

8uqo - Revision history

OCA at 08:06, 6 December 2023

OCA at 09:09, 8 November 2023

OCA: Protected "8uqo" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 8uqo is ON HOLD Authors: Description: Category: Unreleased Structures