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| | <StructureSection load='1vip' size='340' side='right'caption='[[1vip]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1vip' size='340' side='right'caption='[[1vip]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1vip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_russellii Daboia russellii russellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1vip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russelii_russelii Daboia russelii russelii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://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=SO4:SULFATE+ION'>SO4</scene></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=1vip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vip OCA], [https://pdbe.org/1vip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vip RCSB], [https://www.ebi.ac.uk/pdbsum/1vip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vip 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=1vip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vip OCA], [https://pdbe.org/1vip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vip RCSB], [https://www.ebi.ac.uk/pdbsum/1vip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vip ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PA2B_DABRR PA2B_DABRR]] Snake venom phospholipase A2 (PLA2) that has low enzymatic activity, is devoid of lethal activity but has strong anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:8835338</ref>
| + | [https://www.uniprot.org/uniprot/PA2B_DABRR PA2B_DABRR] Snake venom phospholipase A2 (PLA2) that has low enzymatic activity, is devoid of lethal activity but has strong anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:8835338</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Daboia russellii russellii]] | + | [[Category: Daboia russelii russelii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carredano, E]] | + | [[Category: Carredano E]] |
| - | [[Category: Eaker, D]] | + | [[Category: Eaker D]] |
| - | [[Category: Eklund, H]] | + | [[Category: Eklund H]] |
| - | [[Category: Persson, B]] | + | [[Category: Persson B]] |
| - | [[Category: Ramaswamy, S]] | + | [[Category: Ramaswamy S]] |
| - | [[Category: Saarinen, M]] | + | [[Category: Saarinen M]] |
| - | [[Category: Westerlund, B]] | + | [[Category: Westerlund B]] |
| - | [[Category: Anticoagulant]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phospholipase a2]]
| + | |
| Structural highlights
Function
PA2B_DABRR Snake venom phospholipase A2 (PLA2) that has low enzymatic activity, is devoid of lethal activity but has strong anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1]
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 three-dimensional structures of the class II anticoagulant phospholipase A2 (PLA2) toxin RVV-VD from the venom of Russell's viper, Vipera russelli russelli, and the class I neurotoxic PLA2 Notechis II-5 from the, Australian tiger snake, Notechis scutatus scutatus, were determined to 2.2 A and 3.0 A resolution, respectively. Both enzymes are monomeric and consist of 121 and 119 residues, respectively. A comparison of ten class I/II PLA2 structures showed, among other differences, that the beta-sheet of these enzymes (residues 76-83) is about 90 degrees less twisted in class I than in class II PLA2s. This, along with the insertion of some residues in the region 57-59 in class I enzymes (the elapid loop), could be the main reason for the significant difference in the anticoagulant and (presynaptic) neurotoxic properties between the two classes of PLA2. It seems apparent from sequence and structural comparisons that the toxic site of PLA2 responsible for the strong anticoagulancy of these toxins consists of a negatively charged part, Glu53, together with a positively charged ridge of lysine residues free for intermolecular interactions. These lysines differ between the two classes of PLA2.
The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2.,Carredano E, Westerlund B, Persson B, Saarinen M, Ramaswamy S, Eaker D, Eklund H Toxicon. 1998 Jan;36(1):75-92. PMID:9604284[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tsai IH, Lu PJ, Su JC. Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies. Toxicon. 1996 Jan;34(1):99-109. PMID:8835338
- ↑ Carredano E, Westerlund B, Persson B, Saarinen M, Ramaswamy S, Eaker D, Eklund H. The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2. Toxicon. 1998 Jan;36(1):75-92. PMID:9604284
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