7rjz
From Proteopedia
(Difference between revisions)
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==BthTX-II variant a, from Bothrops jararacussu venom, complexed with benzoic acid== | ==BthTX-II variant a, from Bothrops jararacussu venom, complexed with benzoic acid== | ||
| - | <StructureSection load='7rjz' size='340' side='right'caption='[[7rjz]]' scene=''> | + | <StructureSection load='7rjz' size='340' side='right'caption='[[7rjz]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RJZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7rjz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_jararacussu Bothrops jararacussu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RJZ FirstGlance]. <br> |
| - | </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=7rjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rjz OCA], [https://pdbe.org/7rjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rjz RCSB], [https://www.ebi.ac.uk/pdbsum/7rjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rjz ProSAT]</span></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]] 1.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</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=7rjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rjz OCA], [https://pdbe.org/7rjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rjz RCSB], [https://www.ebi.ac.uk/pdbsum/7rjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rjz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PA2B2_BOTJR PA2B2_BOTJR] Snake venom phospholipase A2 (PLA2) that shows a moderate enzymatic activity. It induces indirect hemolytic, anticoagulant, and cytotoxic activities. In vivo, it induces muscle necrosis, accompanied by polymorphonuclear cell infiltration, and edema in the mouse paw. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:9619591</ref> <ref>PMID:11018293</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phospholipases A2 (PLA2s) are found in almost every venomous snake family. In snakebites, some PLA2s can quickly cause local myonecrosis, which may lead to permanent sequelae if antivenom is administered belatedly. They hydrolyse phospholipids in membranes through a catalytic calcium ions-dependent mechanism. BthTX-II is a basic PLA2 and the second major component in the venom of Bothrops jararacussu. Herein, using the software SEQUENCE SLIDER, which integrates crystallographic, mass spectrometry and genetic data, we characterized the primary, tertiary and quaternary structure of two BthTX-II variants (called a and b), which diverge in 7 residues. Crystallographic structure BthTX-IIa is in a Tense-state with its distorted calcium binding loop buried in the dimer interface, contrarily, the novel BthTX-IIb structure is a monomer in a Relax-state with a fatty acid in the hydrophobic channel. Structural data in solution reveals that both variants are monomeric in neutral physiological conditions and mostly dimeric in an acidic environment, being catalytic active in both situations. Therefore, we propose two myotoxic mechanisms for BthTX-II, a catalytic one associated with the monomeric assembly, whereas the other has a calcium independent activity related to its C-terminal region, adopting a dimeric conformation similar to PLA2-like proteins. | ||
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| + | BthTX-II from Bothrops jararacussu venom has variants with different oligomeric assemblies: An example of snake venom phospholipases A2 versatility.,Borges RJ, Salvador GHM, Campanelli HB, Pimenta DC, de Oliveira Neto M, Uson I, Fontes MRM Int J Biol Macromol. 2021 Nov 30;191:255-266. doi:, 10.1016/j.ijbiomac.2021.09.083. Epub 2021 Sep 20. PMID:34547312<ref>PMID:34547312</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7rjz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bothrops jararacussu]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Borges RJ]] | [[Category: Borges RJ]] | ||
[[Category: Fontes MRM]] | [[Category: Fontes MRM]] | ||
Revision as of 16:32, 18 October 2023
BthTX-II variant a, from Bothrops jararacussu venom, complexed with benzoic acid
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