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1poa

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[[Image:1poa.gif|left|200px]]
 
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{{Structure
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==INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2==
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|PDB= 1poa |SIZE=350|CAPTION= <scene name='initialview01'>1poa</scene>, resolution 1.5&Aring;
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<StructureSection load='1poa' size='340' side='right'caption='[[1poa]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1poa]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1POA FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1poa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1poa OCA], [https://pdbe.org/1poa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1poa RCSB], [https://www.ebi.ac.uk/pdbsum/1poa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1poa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1poa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1poa ConSurf].
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<div style="clear:both"></div>
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'''INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2'''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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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].
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==Reference==
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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]
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[[Category: Naja atra]]
[[Category: Naja atra]]
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[[Category: Phospholipase A(2)]]
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[[Category: Otwinowski Z]]
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[[Category: Single protein]]
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[[Category: Scott DL]]
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[[Category: Otwinowski, Z.]]
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[[Category: Sigler PB]]
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[[Category: Scott, D L.]]
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[[Category: Sigler, P B.]]
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[[Category: CA]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:53 2008''
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Current revision

INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2

PDB ID 1poa

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