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| <StructureSection load='1fe5' size='340' side='right'caption='[[1fe5]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='1fe5' size='340' side='right'caption='[[1fe5]], [[Resolution|resolution]] 2.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1fe5]] is a 1 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=1FE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FE5 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1fe5]] is a 1 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=1FE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FE5 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]] 2.45Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dpy|1dpy]]</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='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=1fe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fe5 OCA], [https://pdbe.org/1fe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fe5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fe5 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=1fe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fe5 OCA], [http://pdbe.org/1fe5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fe5 RCSB], [http://www.ebi.ac.uk/pdbsum/1fe5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fe5 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/PA2B_BUNCE PA2B_BUNCE] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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=1fe5 ConSurf]. | | </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=1fe5 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| This is the first phospholipase A2 (PLA2) structure from the family of kraits. The protein was isolated from Bungarus caeruleus (common krait) and the primary sequence was determined using cDNA approach. Three-dimensional structure of this presynaptic neurotoxic PLA2 from group I has been determined by molecular replacement method using the model of PLA2 component of beta2-bungarotoxin (Bungarus multicinctus) and refined using CNS package to a final R-factor of 20.1 % for all the data in resolution range 20.0-2.4 A. The final refined model comprises 897 protein atoms and 77 water molecules. The overall framework of krait phospholipase A2 with three long helices and two short antiparallel beta-strands is extremely similar to those observed for other group I PLA2s. However, the critical parts of PLA2 folding are concerned with its various functional loops. The conformations of these loops determine the efficiency of enzyme action and presence/absence of various pharmacological functions. In the present structure calcium-binding loop is occupied by a sodium ion with a 7-fold co-ordination. The conformation of loop 55-75 in krait PLA2 corresponds to a very high activity of the enzyme. A comparison of its sequence with multimeric PLA2s clearly shows the absence of critical residues such as Tyr3, Trp61 and Phe64, which are involved in the multimerization of PLA2 molecules. The protein shows anticoagulant and neurotoxic activities.
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| Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.,Singh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP J Mol Biol. 2001 Apr 6;307(4):1049-59. PMID:11286555<ref>PMID:11286555</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1fe5" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Phospholipase A2|Phospholipase A2]] | | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bungarus caeruleus]] | | [[Category: Bungarus caeruleus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Gourinath, S]] | | [[Category: Gourinath S]] |
| [[Category: Paramasivam, M]] | | [[Category: Paramasivam M]] |
| [[Category: Sharma, S]] | | [[Category: Sharma S]] |
| [[Category: Singh, G]] | | [[Category: Singh G]] |
| [[Category: Singh, T P]] | | [[Category: Singh TP]] |
| [[Category: Srinivasan, A]] | | [[Category: Srinivasan A]] |
| [[Category: Molecular replacement]]
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| [[Category: Neurotoxic site]]
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| [[Category: Presynaptic neurotoxin]]
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| [[Category: Toxin]]
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| [[Category: X-ray structure]]
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