From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1poa.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1poa.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1poa| PDB=1poa | SCENE= }} | | {{STRUCTURE_1poa| PDB=1poa | SCENE= }} |
| | | | |
| - | '''INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_2274785}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2274785 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_2274785}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 26: |
Line 30: |
| | [[Category: Sigler, P B.]] | | [[Category: Sigler, P B.]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:18:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:19:51 2008'' |
Revision as of 11:19, 27 July 2008
Template:STRUCTURE 1poa
INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2
Template:ABSTRACT PUBMED 2274785
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 Sun Jul 27 14:19:51 2008
