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1zl7
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1zl7" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zl7, resolution 1.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1zl7.gif|left|200px]]<br /><applet load="1zl7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1zl7, resolution 1.60Å" /> | ||
| - | '''Crystal structure of catalytically-active phospholipase A2 with bound calcium'''<br /> | ||
| - | == | + | ==Crystal structure of catalytically-active phospholipase A2 with bound calcium== |
| - | The electrophile Ca(2+) is an essential multifunctional co-factor in the | + | <StructureSection load='1zl7' size='340' side='right'caption='[[1zl7]], [[Resolution|resolution]] 1.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1zl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_jararacussu Bothrops jararacussu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZL7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zl7 OCA], [https://pdbe.org/1zl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zl7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PA2A_BOTJR PA2A_BOTJR] Snake venom phospholipase A2 (PLA2) that induces edema (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:12167491</ref> <ref>PMID:15214498</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zl/1zl7_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1zl7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The electrophile Ca(2+) is an essential multifunctional co-factor in the phospholipase A(2) mediated hydrolysis of phospholipids. Crystal structures of an acidic phospholipase A(2) from the venom of Bothrops jararacussu have been determined both in the Ca(2+) free and bound states at 0.97 and 1.60 A resolutions, respectively. In the Ca(2+) bound state, the Ca(2+) ion is penta-coordinated by a distorted pyramidal cage of oxygen and nitrogen atoms that is significantly different to that observed in structures of other Group I/II phospholipases A(2). In the absence of Ca(2+), a water molecule occupies the position of the Ca(2+) ion and the side chain of Asp49 and the calcium-binding loop adopts a different conformation. | ||
| - | + | Insights into metal ion binding in phospholipases A2: ultra high-resolution crystal structures of an acidic phospholipase A2 in the Ca2+ free and bound states.,Murakami MT, Gabdoulkhakov A, Genov N, Cintra AC, Betzel C, Arni RK Biochimie. 2006 May;88(5):543-9. Epub 2005 Dec 5. PMID:16376474<ref>PMID:16376474</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1zl7" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bothrops jararacussu]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arni RK]] | ||
| + | [[Category: Betzel C]] | ||
| + | [[Category: Cintra AC]] | ||
| + | [[Category: Gabdoulkhakov A]] | ||
| + | [[Category: Genov N]] | ||
| + | [[Category: Murakami MT]] | ||
Current revision
Crystal structure of catalytically-active phospholipase A2 with bound calcium
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