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1poa

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Revision as of 23:00, 9 September 2015

INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2

Structural highlights

1poa is a 1 chain structure with sequence from Chinese cobra. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PA2A1_NAJAT] Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Huang LF, Zheng JB, Xu Y, Song HT, Yu CX. A snake venom phospholipase A2 with high affinity for muscarinic acetylcholine receptors acts on guinea pig ileum. Toxicon. 2008 May;51(6):1008-16. doi: 10.1016/j.toxicon.2008.01.006. Epub 2008, Jan 17. PMID:18281071 doi:http://dx.doi.org/10.1016/j.toxicon.2008.01.006
↑ Kini RM, Evans HJ. Structure-function relationships of phospholipases. The anticoagulant region of phospholipases A2. J Biol Chem. 1987 Oct 25;262(30):14402-7. PMID:3117784
↑ Scott DL, White SP, Otwinowski Z, Yuan W, Gelb MH, Sigler PB. Interfacial catalysis: the mechanism of phospholipase A2. Science. 1990 Dec 14;250(4987):1541-6. PMID:2274785

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1poa"

Categories: Chinese cobra | Otwinowski, Z | Scott, D L | Sigler, P B | Hydrolase

@@ Line 2: / Line 2: @@
 <StructureSection load='1poa' size='340' side='right' caption='[[1poa]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1poa]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1POA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1poa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chinese_cobra Chinese cobra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1POA FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1poa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1poa RCSB], [http://www.ebi.ac.uk/pdbsum/1poa PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1poa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poa OCA], [http://pdbe.org/1poa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1poa RCSB], [http://www.ebi.ac.uk/pdbsum/1poa PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PA21_NAJAT PA21_NAJAT]] Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18281071</ref> <ref>PMID:3117784</ref>
+[[http://www.uniprot.org/uniprot/PA2A1_NAJAT PA2A1_NAJAT]] Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18281071</ref> <ref>PMID:3117784</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1poa" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Naja atra]]
+[[Category: Chinese cobra]]
 [[Category: Otwinowski, Z]]
 [[Category: Scott, D L]]
 [[Category: Sigler, P B]]
 [[Category: Hydrolase]]

1poa

From Proteopedia

Revision as of 23:00, 9 September 2015

INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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