6kqu
From Proteopedia
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==Crystal structure of phospholipase A2== | ==Crystal structure of phospholipase A2== | ||
| - | <StructureSection load='6kqu' size='340' side='right'caption='[[6kqu]]' scene=''> | + | <StructureSection load='6kqu' size='340' side='right'caption='[[6kqu]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KQU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6kqu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KQU FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqu OCA], [http://pdbe.org/6kqu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kqu RCSB], [http://www.ebi.ac.uk/pdbsum/6kqu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqu ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5y5e|5y5e]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLA2G2E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqu OCA], [http://pdbe.org/6kqu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kqu RCSB], [http://www.ebi.ac.uk/pdbsum/6kqu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PA2GE_HUMAN PA2GE_HUMAN]] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Secreted phospholipases A2 (sPLA2) group IIE (GIIE) is involved in several biological events, such as lipid metabolism and possibly inflammation that may mainly depend on its catalytic reaction. We previously showed that Asn21 is a critical residue that contributes to the enzymatic activity of hGIIE, but the underlying mechanism is still not clear. Here, combined with crystal structures and mutagenesis studies of the Asn21Gly mutant, we demonstrate that Asn21 acts as a switch responsible for the calcium binding and the catalytic efficiency. Our results of the atypical feature of calcium binding in hGIIE not only provide clues to understand the molecular basis of its enzymatic activity and physiological function, but also confer improved specificity for potential inhibitor design of sPLA2. | ||
| + | |||
| + | Residue Asn21 acts as a switch for calcium binding to modulate the enzymatic activity of human phospholipase A2 group IIE.,Hou S, Zhang Y, Xu J, Bai J, Liu J, Xie J, Xu T Biochimie. 2020 Sep;176:117-121. doi: 10.1016/j.biochi.2020.07.003. Epub 2020 Jul, 10. PMID:32659444<ref>PMID:32659444</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6kqu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hou S]] | + | [[Category: Hou, S]] |
| - | [[Category: Liu J]] | + | [[Category: Liu, J]] |
| - | [[Category: Xu T]] | + | [[Category: Xu, T]] |
| + | [[Category: Calcium]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Mutation]] | ||
| + | [[Category: Phospholipase a2]] | ||
Revision as of 09:48, 9 September 2020
Crystal structure of phospholipase A2
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Categories: Human | Large Structures | Hou, S | Liu, J | Xu, T | Calcium | Hydrolase | Mutation | Phospholipase a2
