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| | ==PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, 18 STRUCTURES== | | ==PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, 18 STRUCTURES== |
| - | <StructureSection load='1sfw' size='340' side='right'caption='[[1sfw]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | + | <StructureSection load='1sfw' size='340' side='right'caption='[[1sfw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sfw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SFW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sfw]] 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=1SFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SFW FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 18 models</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sfv|1sfv]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PORCINE PANCREAS PLA2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfw OCA], [https://pdbe.org/1sfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sfw RCSB], [https://www.ebi.ac.uk/pdbsum/1sfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfw ProSAT]</span></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=1sfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfw OCA], [https://pdbe.org/1sfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sfw RCSB], [https://www.ebi.ac.uk/pdbsum/1sfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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.
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sf/1sfw_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sf/1sfw_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <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> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pig]] | + | [[Category: Sus scrofa]] |
| - | [[Category: Berg, B Van Den]] | + | [[Category: Boelens R]] |
| - | [[Category: Boelens, R]] | + | [[Category: De Haas GH]] |
| - | [[Category: Dijkman, R]] | + | [[Category: Dijkman R]] |
| - | [[Category: Haas, G H.De]]
| + | [[Category: Kaptein R]] |
| - | [[Category: Kaptein, R]] | + | [[Category: Tessari M]] |
| - | [[Category: Tessari, M]] | + | [[Category: Van Den Berg B]] |
| - | [[Category: Verheij, H M]] | + | [[Category: Verheij HM]] |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Phosphatide-2-acyl-hydrolase]]
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| - | [[Category: Phospholipase a2]]
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| Structural highlights
Function
PA21B_PIG PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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 PubMed
The three-dimensional structure of porcine pancreatic PLA2 (PLA2), present in a 40 kDa ternary complex with micelles and a competitive inhibitor, has been determined using multidimensional heteronuclear NMR spectroscopy. The structure of the protein (124 residues) is based on 1854 constraints, comprising 1792 distance and 62 phi torsion angle constraints. A total of 18 structures was calculated using a combined approach of distance geometry and restrained molecular dynamics. The atomic rms distribution about the mean coordinate positions for residues 1-62 and 72-124 is 0.75 +/- 0.09 A for the backbone atoms and 1.14 +/- 0.10 A for all atoms. The rms difference between the averaged minimized NMR structures of the free PLA2 and PLA2 in the ternary complex is 3.5 A for the backbone atoms and 4.0 A for all atoms. Large differences occur for the calcium-binding loop and the surface loop from residues 62 through 72. The most important difference is found for the first three residues of the N-terminal alpha-helix. Whereas free in solution Ala1, Leu2 and Trp3 are disordered, with the alpha-helical conformation with the alpha-amino group buried inside the protein. As a consequence, the important conserved hydrogen bonding network which is also seen in the crystal structures is present only in the ternary complex, but not in free PLA2. Thus, the NMR structure of the N-terminal region (as well as the calcium-binding loop and the surface loop) of PLA2 in the ternary complex resembles that of the crystal structure. Comparison of the NMR structures of the free enzyme and the enzyme in the ternary complex indicates that conformational changes play a role in the interfacial activation of PLA2.
Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor.,van den Berg B, Tessari M, Boelens R, Dijkman R, Kaptein R, de Haas GH, Verheij HM J Biomol NMR. 1995 Feb;5(2):110-21. PMID:7703697[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ van den Berg B, Tessari M, Boelens R, Dijkman R, Kaptein R, de Haas GH, Verheij HM. Solution structure of porcine pancreatic phospholipase A2 complexed with micelles and a competitive inhibitor. J Biomol NMR. 1995 Feb;5(2):110-21. PMID:7703697
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