3elo

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(New page: '''Unreleased structure''' The entry 3elo is ON HOLD Authors: Xu, W., Yi, L., Feng, Y., Chen, L., Liu, J. Description: Crystal Structure of Human Pancreatic Prophospholipase A2 ''Page...)
Current revision (11:52, 16 February 2022) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3elo is ON HOLD
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==Crystal Structure of Human Pancreatic Prophospholipase A2==
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<StructureSection load='3elo' size='340' side='right'caption='[[3elo]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3elo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ELO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ELO 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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLA2G1B ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr>
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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=3elo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3elo OCA], [https://pdbe.org/3elo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3elo RCSB], [https://www.ebi.ac.uk/pdbsum/3elo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3elo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/PA21B_HUMAN PA21B_HUMAN]] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules.<ref>PMID:19297324</ref>
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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/el/3elo_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=3elo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pancreatic phospholipase A2 (phospholipase A2 group 1B, G1B) belongs to the superfamily of secreted phospholipase A2 (PLA2) enzymes. G1B has been proposed to be a potential target for diseases such as hypertension, obesity, and diabetes. Human pancreatic prophospholipase A2 (pro-hG1B) is activated by cleavage of the first seven-residue propeptide (phospholipase A2 propeptide, PROP). However, questions still remain on the mode of action for pro-hG1B. In this work, we expressed pro-hG1B in Pichia pastoris and determined the crystal structure at 1.55-A resolution. The x-ray structure demonstrates that pro-hG1B forms a trimer. In addition, PROP occupies the catalytic cavity and can be self-cleaved at 37 degrees C. A new membrane-bound surface and activation mechanism are proposed based on the trimeric model of pro-hG1B. We also propose a new autoproteolytic mechanism for pro-hG1B by the reaction triad Asp49-Arg0-Ser(-2) that is similar to the serine protease catalytic triad.
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Authors: Xu, W., Yi, L., Feng, Y., Chen, L., Liu, J.
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Structural insight into the activation mechanism of human pancreatic prophospholipase A2.,Xu W, Yi L, Feng Y, Chen L, Liu J J Biol Chem. 2009 Jun 12;284(24):16659-66. Epub 2009 Mar 18. PMID:19297324<ref>PMID:19297324</ref>
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Description: Crystal Structure of Human Pancreatic Prophospholipase A2
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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 3elo" style="background-color:#fffaf0;"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 1 21:14:23 2008''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Chen, L]]
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[[Category: Feng, Y]]
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[[Category: Liu, J]]
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[[Category: Xu, W]]
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[[Category: Yi, L]]
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[[Category: Human pancreatic prophospholipase a2]]
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[[Category: Hydrolase]]
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[[Category: Lipid degradation]]
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[[Category: Metal-binding]]
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[[Category: Secreted]]
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[[Category: Trimeric]]

Current revision

Crystal Structure of Human Pancreatic Prophospholipase A2

PDB ID 3elo

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