1sfv: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:


==PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE==
==PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE==
<StructureSection load='1sfv' size='340' side='right'caption='[[1sfv]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1sfv' size='340' side='right'caption='[[1sfv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sfv]] 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=1SFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SFV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sfv]] 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=1SFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SFV 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</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sfw|1sfw]]</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>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfv OCA], [https://pdbe.org/1sfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sfv RCSB], [https://www.ebi.ac.uk/pdbsum/1sfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfv 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=1sfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfv OCA], [https://pdbe.org/1sfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sfv RCSB], [https://www.ebi.ac.uk/pdbsum/1sfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfv 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]]
Line 22: Line 20:
</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=1sfv ConSurf].
</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=1sfv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:7703697</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1sfv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</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]]
[[Category: Phospholipase a2]]

Revision as of 08:31, 1 May 2024

PORCINE PANCREAS PHOSPHOLIPASE A2, NMR, MINIMIZED AVERAGE STRUCTURE

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1sfv&oldid=4140355"