1pir
From Proteopedia
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|PDB= 1pir |SIZE=350|CAPTION= <scene name='initialview01'>1pir</scene> | |PDB= 1pir |SIZE=350|CAPTION= <scene name='initialview01'>1pir</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1pis|1PIS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pir OCA], [http://www.ebi.ac.uk/pdbsum/1pir PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pir RCSB]</span> | ||
}} | }} | ||
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[[Category: Tessari, M.]] | [[Category: Tessari, M.]] | ||
[[Category: Verheij, H M.]] | [[Category: Verheij, H M.]] | ||
| - | [[Category: CA]] | ||
[[Category: phosphatide-2-acyl-hydrolase]] | [[Category: phosphatide-2-acyl-hydrolase]] | ||
[[Category: phospholipase a2]] | [[Category: phospholipase a2]] | ||
[[Category: pla2]] | [[Category: pla2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:10 2008'' |
Revision as of 20:00, 30 March 2008
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| Ligands: | |||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Related: | 1PIS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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