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| | <StructureSection load='1poa' size='340' side='right'caption='[[1poa]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1poa' size='340' side='right'caption='[[1poa]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1poa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ansp_6988 Ansp 6988]. 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 [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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1poa ProSAT]</span></td></tr> | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1poa_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1poa_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | ==See Also== | | ==See Also== |
| - | *[[Phospholipase A2|Phospholipase A2]] | + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ansp 6988]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Otwinowski, Z]] | + | [[Category: Naja atra]] |
| - | [[Category: Scott, D L]] | + | [[Category: Otwinowski Z]] |
| - | [[Category: Sigler, P B]] | + | [[Category: Scott DL]] |
| - | [[Category: Hydrolase]] | + | [[Category: Sigler PB]] |
| Structural highlights
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.
See Also
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
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