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| | <StructureSection load='1qll' size='340' side='right'caption='[[1qll]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='1qll' size='340' side='right'caption='[[1qll]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qll]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bothrops_pirajai Bothrops pirajai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QLL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qll]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_pirajai Bothrops pirajai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QLL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TDA:N-TRIDECANOIC+ACID'>TDA</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]] 2.04Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1clp|1clp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TDA:N-TRIDECANOIC+ACID'>TDA</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=1qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qll OCA], [https://pdbe.org/1qll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qll RCSB], [https://www.ebi.ac.uk/pdbsum/1qll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qll ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qll OCA], [http://pdbe.org/1qll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qll RCSB], [http://www.ebi.ac.uk/pdbsum/1qll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qll ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PA2H2_BOTPI PA2H2_BOTPI]] Snake venom phospholipase A2 (PLA2) homolog that lacks enzymatic activity, but has myotoxic activity and edema-inducing activities in vivo.<ref>PMID:10863008</ref> | + | [https://www.uniprot.org/uniprot/PA2H2_BOTPI PA2H2_BOTPI] Snake venom phospholipase A2 (PLA2) homolog that lacks enzymatic activity, but has myotoxic activity and edema-inducing activities in vivo.<ref>PMID:10863008</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bothrops pirajai]] | | [[Category: Bothrops pirajai]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lee, W H]] | + | [[Category: Lee W-H]] |
| - | [[Category: Polikarpov, I]] | + | [[Category: Polikarpov I]] |
| - | [[Category: Neurotoxin]]
| + | |
| Structural highlights
Function
PA2H2_BOTPI Snake venom phospholipase A2 (PLA2) homolog that lacks enzymatic activity, but has myotoxic activity and edema-inducing activities in vivo.[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
Asp49 plays a fundamental role in supporting catalysis by phospholipases A2 by coordinating the calcium ion which aids in the stabilization of the tetrahedral intermediate. In several myotoxins from the venoms of Viperidae snakes, this aspartic acid is substituted by lysine. The loss of calcium binding capacity by these mutants has become regarded as the standard explanation for their greatly reduced or nonexistent phospholipolytic activity. Here we describe the crystal structure of one such Lys49 PLA2, piratoxin-II, in which a fatty acid molecule is observed within the substrate channel. This suggests that such toxins may be active enzymes in which catalysis is interrupted at the stage of substrate release. Comparison of the present structure with other PLA2s, both active and inactive, identifies Lys122 as one of the likely causes of the increased affinity for fatty acid in Lys49 enzymes. Its interaction with the mainchain carbonyl of Cys29 is expected to lead to hyperpolarization of the peptide bond between residues 29 and 30 leading to an increased affinity for the fatty acid headgroup. This strongly bound fatty acid may serve as an anchor to secure the toxin within the membrane thus facilitating its pathological effects.
Structural basis for low catalytic activity in Lys49 phospholipases A2--a hypothesis: the crystal structure of piratoxin II complexed to fatty acid.,Lee WH, da Silva Giotto MT, Marangoni S, Toyama MH, Polikarpov I, Garratt RC Biochemistry. 2001 Jan 9;40(1):28-36. PMID:11141053[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Toyama MH, Soares AM, Wen-Hwa L, Polikarpov I, Giglio JR, Marangoni S. Amino acid sequence of piratoxin-II, a myotoxic lys49 phospholipase A(2) homologue from Bothrops pirajai venom. Biochimie. 2000 Mar;82(3):245-50. PMID:10863008
- ↑ Lee WH, da Silva Giotto MT, Marangoni S, Toyama MH, Polikarpov I, Garratt RC. Structural basis for low catalytic activity in Lys49 phospholipases A2--a hypothesis: the crystal structure of piratoxin II complexed to fatty acid. Biochemistry. 2001 Jan 9;40(1):28-36. PMID:11141053
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