1pir
From Proteopedia
(New page: 200px<br /><applet load="1pir" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pir" /> '''SOLUTION STRUCTURE OF PORCINE PANCREATIC PHO...) |
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'''SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2'''<br /> | '''SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The lipolytic enzyme phospholipase A2 (PLA2) is involved in the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1PIR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1PIR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Berg, B | + | [[Category: Berg, B D.Van Den.]] |
[[Category: Boelens, R.]] | [[Category: Boelens, R.]] | ||
| - | [[Category: Haas, G | + | [[Category: Haas, G H.De.]] |
[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: Tessari, M.]] | [[Category: Tessari, M.]] | ||
| - | [[Category: Verheij, H | + | [[Category: Verheij, H M.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: phosphatide-2-acyl-hydrolase]] | [[Category: phosphatide-2-acyl-hydrolase]] | ||
| Line 25: | Line 25: | ||
[[Category: pla2]] | [[Category: pla2]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:09 2008'' |
Revision as of 12:29, 21 February 2008
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SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2
Overview
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.
About this Structure
1PIR is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from 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:7556053
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