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| | <StructureSection load='1g2x' size='340' side='right'caption='[[1g2x]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1g2x' size='340' side='right'caption='[[1g2x]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g2x]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_caeruleus Bungarus caeruleus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G2X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g2x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_caeruleus Bungarus caeruleus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G2X FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fe5|1fe5]], [[1g0z|1g0z]]</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]] 2.5Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2x OCA], [https://pdbe.org/1g2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g2x RCSB], [https://www.ebi.ac.uk/pdbsum/1g2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2x ProSAT]</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=1g2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2x OCA], [http://pdbe.org/1g2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g2x RCSB], [http://www.ebi.ac.uk/pdbsum/1g2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PA2B3_BUNCE PA2B3_BUNCE] Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). |
| | == 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/g2/1g2x_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/1g2x_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/> |
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| | [[Category: Bungarus caeruleus]] | | [[Category: Bungarus caeruleus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhanumathi, S]] | + | [[Category: Bhanumathi S]] |
| - | [[Category: Gourinath, S]] | + | [[Category: Gourinath S]] |
| - | [[Category: Paramsivam, M]] | + | [[Category: Paramsivam M]] |
| - | [[Category: Sharma, S]] | + | [[Category: Sharma S]] |
| - | [[Category: Singh, G]] | + | [[Category: Singh G]] |
| - | [[Category: Singh, T P]] | + | [[Category: Singh TP]] |
| - | [[Category: Homotrimer]]
| + | |
| - | [[Category: Phospholipase a2]]
| + | |
| - | [[Category: Toxin]]
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| Structural highlights
Function
PA2B3_BUNCE Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).
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
The venom of the common Indian krait (Bungarus caeruleus) contains about a dozen isoforms of phospholipase A2 (PLA2), which exist in different oligomeric forms as well as in complexes with low-molecular-weight ligands. The basic objective of multimerization and complexation is either to inactivate PLA2 in the venom for long-term storage, to generate a new PLA2 function or to make a more lethal assembly. The current isoform was isolated from the venom of B. caeruleus. Dynamic light-scattering studies indicated the presence of a stable trimeric association of this PLA2. Its primary sequence was determined by cDNA cloning. The purified protein was crystallized with 2.8 M NaCl as a precipitating agent using the sitting-drop vapour-diffusion method. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 80.9, b = 80.5, c = 57.1 A, beta = 90.3 degrees. The structure was refined to a final R factor of 0.198. This is a novel trimeric PLA2 structure in which the central pore formed by the association of three molecules is filled with water molecules. The interactions across the pore take place via multiple water bridges primarily to the side chains of Arg, Lys and Thr residues. Approximately 12% of the total solvent-accessible surface area is buried in the core of the trimer. The active sites of all three molecules are located on the surface and are fully exposed to the solvent, resulting in a highly potent enzymatic unit.
Sequence-induced trimerization of phospholipase A2: structure of a trimeric isoform of PLA2 from common krait (Bungarus caeruleus) at 2.5 A resolution.,Singh G, Gourinath S, Saravanan K, Sharma S, Bhanumathi S, Betzel Ch, Srinivasan A, Singh TP Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):8-13. Epub 2004 Oct 16. PMID:16508078[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Singh G, Gourinath S, Saravanan K, Sharma S, Bhanumathi S, Betzel Ch, Srinivasan A, Singh TP. Sequence-induced trimerization of phospholipase A2: structure of a trimeric isoform of PLA2 from common krait (Bungarus caeruleus) at 2.5 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):8-13. Epub 2004 Oct 16. PMID:16508078 doi:http://dx.doi.org/10.1107/S1744309104025503
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