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[[Image:3p2p.jpg|left|200px]]
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{{STRUCTURE_3p2p|  PDB=3p2p  |  SCENE=  }}
'''ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP'''


==ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP==
<StructureSection load='3p2p' size='340' side='right'caption='[[3p2p]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3p2p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P2P 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]] 2.1&#8491;</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></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=3p2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2p OCA], [https://pdbe.org/3p2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p2p RCSB], [https://www.ebi.ac.uk/pdbsum/3p2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p2p 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/p2/3p2p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3p2p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.


==Overview==
Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop.,Kuipers OP, Thunnissen MM, de Geus P, Dijkstra BW, Drenth J, Verheij HM, de Haas GH Science. 1989 Apr 7;244(4900):82-5. PMID:2704992<ref>PMID:2704992</ref>
Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3P2P 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=3P2P OCA].
</div>
<div class="pdbe-citations 3p2p" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop., Kuipers OP, Thunnissen MM, de Geus P, Dijkstra BW, Drenth J, Verheij HM, de Haas GH, Science. 1989 Apr 7;244(4900):82-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2704992 2704992]
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Dijkstra, B W.]]
[[Category: Dijkstra BW]]
[[Category: Drenth, J.]]
[[Category: Drenth J]]
[[Category: Kalk, K H.]]
[[Category: Kalk KH]]
[[Category: Thunnissen, M M.G M.]]
[[Category: Thunnissen MMGM]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:08:41 2008''

Latest revision as of 09:32, 30 October 2024

ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP

3p2p, resolution 2.10Å

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