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[[Image:1pis.gif|left|200px]]


{{Structure
==SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2==
|PDB= 1pis |SIZE=350|CAPTION= <scene name='initialview01'>1pis</scene>
<StructureSection load='1pis' size='340' side='right'caption='[[1pis]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[1pis]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PIS FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1pis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pis OCA], [https://pdbe.org/1pis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pis RCSB], [https://www.ebi.ac.uk/pdbsum/1pis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pis ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PA21B_PIG PA21B_PIG] PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
== 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/pi/1pis_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=1pis ConSurf].
<div style="clear:both"></div>


'''SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2'''
==See Also==
 
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The lipolytic enzyme phospholipase A2 (PLA2) is involved in the degradation of high-molecular weight phospholipid aggregates in vivo. The enzyme has very high catalytic activities on aggregated substrates compared with monomeric substrates, a phenomenon called interfacial activation. Crystal structures of PLA2s in the absence and presence of inhibitors are identical, from which it has been concluded that enzymatic conformational changes do not play a role in the mechanism of interfacial activation. The high-resolution NMR structure of porcine pancreatic PLA2 free in solution was determined with heteronuclear multidimensional NMR methodology using doubly labeled 13C, 15N-labeled protein. The solution structure of PLA2 shows important deviations from the crystal structure. In the NMR structure the Ala1 alpha-amino group is disordered and the hydrogen bonding network involving the N-terminus and the active site is incomplete. The disorder observed for the N-terminal region of PLA2 in the solution structure could be related to the low activity of the enzyme towards monomeric substrates. The NMR structure of PLA2 suggests, in contrast to the crystallographic work, that conformational changes do play a role in the interfacial activation of this enzyme.
[[Category: Large Structures]]
 
==About this Structure==
1PIS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIS OCA].
 
==Reference==
Solution structure of porcine pancreatic phospholipase A2., van den Berg B, Tessari M, de Haas GH, Verheij HM, Boelens R, Kaptein R, EMBO J. 1995 Sep 1;14(17):4123-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7556053 7556053]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Berg, B D.Van Den.]]
[[Category: Boelens R]]
[[Category: Boelens, R.]]
[[Category: De Haas GH]]
[[Category: Haas, G H.De.]]
[[Category: Kaptein R]]
[[Category: Kaptein, R.]]
[[Category: Tessari M]]
[[Category: Tessari, M.]]
[[Category: Van Den Berg BD]]
[[Category: Verheij, H M.]]
[[Category: Verheij HM]]
[[Category: CA]]
[[Category: phosphatide-2-acyl-hydrolase]]
[[Category: phospholipase a2]]
[[Category: pla2]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:24:52 2008''
Retrieved from "https://proteopedia.org/1pis"