3qr0

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Current revision (11:55, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qr0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sepia_officinalis Sepia officinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qr0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sepia_officinalis Sepia officinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qr1|3qr1]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3qr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr0 OCA], [https://pdbe.org/3qr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr0 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr0 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=3qr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr0 OCA], [https://pdbe.org/3qr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr0 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr0 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F2YQ19_SEPOF F2YQ19_SEPOF] 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.[PIRNR:PIRNR000956]
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The enzyme phospholipase C-beta (PLCbeta) is a crucial regulator of intracellular calcium levels whose activity is controlled by heptahelical receptors that couple to members of the G(q) family of heterotrimeric G proteins. We have determined atomic structures of two invertebrate homologs of PLCbeta (PLC21) from cephalopod retina and identified a helix from the C-terminal regulatory region that interacts with a conserved surface of the catalytic core of the enzyme. Mutations designed to disrupt the analogous interaction in human PLCbeta3 considerably increase basal activity and diminish stimulation by Galpha(q). Galpha(q) binding requires displacement of the autoinhibitory helix from the catalytic core, thus providing an allosteric mechanism for activation of PLCbeta.
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An autoinhibitory helix in the C-terminal region of phospholipase C-beta mediates Galpha(q) activation.,Lyon AM, Tesmer VM, Dhamsania VD, Thal DM, Gutierrez J, Chowdhury S, Suddala KC, Northup JK, Tesmer JJ Nat Struct Mol Biol. 2011 Aug 7;18(9):999-1005. doi: 10.1038/nsmb.2095. PMID:21822282<ref>PMID:21822282</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qr0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Phospholipase C|Phospholipase C]]
*[[Phospholipase C|Phospholipase C]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sepia officinalis]]
[[Category: Sepia officinalis]]
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[[Category: Lyon, A M]]
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[[Category: Lyon AM]]
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[[Category: Northup, J K]]
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[[Category: Northup JK]]
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[[Category: Tesmer, J J.G]]
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[[Category: Tesmer JJG]]
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[[Category: C2 domain]]
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[[Category: Calcium binding]]
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[[Category: Ef hand]]
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[[Category: Hydrolase]]
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[[Category: Ph domain]]
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[[Category: Phospholipase]]
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[[Category: Phospholipid binding]]
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[[Category: Tim barrel domain]]
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Current revision

Crystal Structure of S. officinalis PLC21

PDB ID 3qr0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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