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==Crystal structure of catalytically-active phospholipase A2 in the absence of calcium== | ==Crystal structure of catalytically-active phospholipase A2 in the absence of calcium== | ||
<StructureSection load='1zlb' size='340' side='right' caption='[[1zlb]], [[Resolution|resolution]] 0.97Å' scene=''> | <StructureSection load='1zlb' size='340' side='right'caption='[[1zlb]], [[Resolution|resolution]] 0.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1zlb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1zlb]] 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=1ZLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZLB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.97Å</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=1zlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zlb OCA], [https://pdbe.org/1zlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zlb RCSB], [https://www.ebi.ac.uk/pdbsum/1zlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zlb ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zl/1zlb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zl/1zlb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 31: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Phospholipase A2|Phospholipase A2]] | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bothrops jararacussu]] | ||
[[Category: Arni | [[Category: Large Structures]] | ||
[[Category: Betzel | [[Category: Arni RK]] | ||
[[Category: Cintra | [[Category: Betzel C]] | ||
[[Category: Gabdoulkhakov | [[Category: Cintra AC]] | ||
[[Category: Genov | [[Category: Gabdoulkhakov A]] | ||
[[Category: Murakami | [[Category: Genov N]] | ||
[[Category: Murakami MT]] | |||
Latest revision as of 10:32, 9 October 2024
Crystal structure of catalytically-active phospholipase A2 in the absence of calciumCrystal structure of catalytically-active phospholipase A2 in the absence of calcium
Structural highlights
FunctionPA2A_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.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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