1umv

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of an acidic, non-myotoxic phospholipase A2 from the venom of Bothrops jararacussu

Structural highlights

1umv is a 1 chain structure with sequence from Bothrops jararacussu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.79Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PA2A_BOTJR Snake venom phospholipase A2 (PLA2) that induces edema (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.^[1] ^[2]

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

Phospholipases A2 belong to the superfamily of proteins which hydrolyzes the sn-2 acyl groups of membrane phospholipids to release arachidonic acid and lysophospholipids. An acidic phospholipase A2 isolated from Bothrops jararacussu snake venom presents a high catalytic, platelet aggregation inhibition and hypotensive activities. This protein was crystallized in two oligomeric states: monomeric and dimeric. The crystal structures were solved at 1.79 and 1.90 angstroms resolution, respectively, for the two states. It was identified a Na+ ion at the center of Ca2+-binding site of the monomeric form. A novel dimeric conformation with the active sites exposed to the solvent was observed. Conformational states of the molecule may be due to the physicochemical conditions used in the crystallization experiments. We suggest dimeric state is one found in vivo.

Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state.,Magro AJ, Murakami MT, Marcussi S, Soares AM, Arni RK, Fontes MR Biochem Biophys Res Commun. 2004 Oct 8;323(1):24-31. PMID:15351695^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Andriao-Escarso SH, Soares AM, Fontes MR, Fuly AL, Correa FM, Rosa JC, Greene LJ, Giglio JR. Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom. Biochem Pharmacol. 2002 Aug 15;64(4):723-32. PMID:12167491
↑ Roberto PG, Kashima S, Marcussi S, Pereira JO, Astolfi-Filho S, Nomizo A, Giglio JR, Fontes MR, Soares AM, Franca SC. Cloning and identification of a complete cDNA coding for a bactericidal and antitumoral acidic phospholipase A2 from Bothrops jararacussu venom. Protein J. 2004 May;23(4):273-85. PMID:15214498
↑ Magro AJ, Murakami MT, Marcussi S, Soares AM, Arni RK, Fontes MR. Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state. Biochem Biophys Res Commun. 2004 Oct 8;323(1):24-31. PMID:15351695 doi:10.1016/j.bbrc.2004.08.046

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1umv"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1umv]] is a 1 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=1UMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMV FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1god|1god]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1umv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umv OCA], [https://pdbe.org/1umv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umv RCSB], [https://www.ebi.ac.uk/pdbsum/1umv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PA2A_BOTJR PA2A_BOTJR]] Snake venom phospholipase A2 (PLA2) that induces edema (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:12167491</ref> <ref>PMID:15214498</ref>
+[https://www.uniprot.org/uniprot/PA2A_BOTJR PA2A_BOTJR] Snake venom phospholipase A2 (PLA2) that induces edema (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:12167491</ref> <ref>PMID:15214498</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1umv_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>
   </jmolCheckbox>
@@ Line 38: / Line 38: @@
 [[Category: Bothrops jararacussu]]
 [[Category: Large Structures]]
-[[Category: Arni, R K]]
+[[Category: Arni RK]]
-[[Category: Cintra, A C.O]]
+[[Category: Cintra ACO]]
-[[Category: Murakami, M T]]
+[[Category: Murakami MT]]
-[[Category: Watanabe, L]]
+[[Category: Watanabe L]]
-[[Category: Acidic]]
-[[Category: Lipase]]
-[[Category: Non-myotoxic]]
-[[Category: Pla2]]

1umv

From Proteopedia

Current revision

Crystal structure of an acidic, non-myotoxic phospholipase A2 from the venom of Bothrops jararacussu

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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