1poa
From Proteopedia
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| - | [[Image:1poa.gif|left|200px]] | + | [[Image:1poa.gif|left|200px]] |
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| - | '''INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2''' | + | {{Structure |
| + | |PDB= 1poa |SIZE=350|CAPTION= <scene name='initialview01'>1poa</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1POA is a [ | + | 1POA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POA OCA]. |
==Reference== | ==Reference== | ||
| - | Interfacial catalysis: the mechanism of phospholipase A2., Scott DL, White SP, Otwinowski Z, Yuan W, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1541-6. PMID:[http:// | + | Interfacial catalysis: the mechanism of phospholipase A2., Scott DL, White SP, Otwinowski Z, Yuan W, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1541-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2274785 2274785] |
[[Category: Naja atra]] | [[Category: Naja atra]] | ||
[[Category: Phospholipase A(2)]] | [[Category: Phospholipase A(2)]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:53 2008'' |
Revision as of 11:26, 20 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2
Overview
A chemical description of the action of phospholipase A2 (PLA2) can now be inferred with confidence from three high-resolution x-ray crystal structures. The first is the structure of the PLA2 from the venom of the Chinese cobra (Naja naja atra) in a complex with a phosphonate transition-state analogue. This enzyme is typical of a large, well-studied homologous family of PLA2S. The second is a similar complex with the evolutionarily distant bee-venom PLA2. The third structure is the uninhibited PLA2 from Chinese cobra venom. Despite the different molecular architectures of the cobra and bee-venom PLA2s, the transition-state analogue interacts in a nearly identical way with the catalytic machinery of both enzymes. The disposition of the fatty-acid side chains suggests a common access route of the substrate from its position in the lipid aggregate to its productive interaction with the active site. Comparison of the cobra-venom complex with the uninhibited enzyme indicates that optimal binding and catalysis at the lipid-water interface is due to facilitated substrate diffusion from the interfacial binding surface to the catalytic site rather than an allosteric change in the enzyme's structure. However, a second bound calcium ion changes its position upon the binding of the transition-state analogue, suggesting a mechanism for augmenting the critical electrophile.
About this Structure
1POA is a Single protein structure of sequence from Naja atra. Full crystallographic information is available from OCA.
Reference
Interfacial catalysis: the mechanism of phospholipase A2., Scott DL, White SP, Otwinowski Z, Yuan W, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1541-6. PMID:2274785
Page seeded by OCA on Thu Mar 20 13:26:53 2008
