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New page: left|200px<br /><applet load="1pc9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pc9, resolution 2.5Å" /> '''Crystal Structure of ... |
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== | ==Crystal Structure of BnSP-6, a Lys49-Phospholipase A2== | ||
Phospholipases A(2) are components of Bothrops venoms responsible for | <StructureSection load='1pc9' size='340' side='right'caption='[[1pc9]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1pc9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_pauloensis Bothrops pauloensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PC9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=1pc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pc9 OCA], [https://pdbe.org/1pc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pc9 RCSB], [https://www.ebi.ac.uk/pdbsum/1pc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pc9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PA2H_BOTPA PA2H_BOTPA] Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity. Is myotoxic. Displays bactericidal activity and promotes the blockage of the neuromuscular contraction of the chick biventer cervicis muscle. Also disrupts artificial membranes, and provokes tissue damages characterized by edema, necrosis and inflammation. May act as pro-inflammatory mediators, inducing metalloproteinase and cytokine production from the inflammatory and satellite cells.<ref>PMID:10860537</ref> <ref>PMID:9972319</ref> <ref>PMID:14623331</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pc9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1pc9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent. | |||
Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights.,Magro AJ, Soares AM, Giglio JR, Fontes MR Biochem Biophys Res Commun. 2003 Nov 21;311(3):713-20. PMID:14623331<ref>PMID:14623331</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1pc9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phospholipase A2 homolog|Phospholipase A2 homolog]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bothrops pauloensis]] | |||
[[Category: Large Structures]] | |||
[[Category: Fontes MRM]] | |||
[[Category: Giglio JR]] | |||
[[Category: Magro AJ]] | |||
[[Category: Soares AM]] | |||
Latest revision as of 11:43, 6 November 2024
Crystal Structure of BnSP-6, a Lys49-Phospholipase A2Crystal Structure of BnSP-6, a Lys49-Phospholipase A2
Structural highlights
FunctionPA2H_BOTPA Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity. Is myotoxic. Displays bactericidal activity and promotes the blockage of the neuromuscular contraction of the chick biventer cervicis muscle. Also disrupts artificial membranes, and provokes tissue damages characterized by edema, necrosis and inflammation. May act as pro-inflammatory mediators, inducing metalloproteinase and cytokine production from the inflammatory and satellite cells.[1] [2] [3] 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 PubMedPhospholipases A(2) are components of Bothrops venoms responsible for disruption of cell membrane integrity via hydrolysis of its phospholipids. A class of PLA(2)-like proteins has been described which despite PLA(2) activity on artificial substrate, due to a D49K mutation, is still highly myonecrotic. This work reports the X-ray structure determination of two Lys49-PLA(2)s from Bothrops neuwiedi pauloensis (BnSP-7 and BnSP-6) and, for the first time, the comparison of eight dimeric Lys49-PLA(2)s. This comparison reveals that there are not just two ("open" and "closed") but at least six different conformations. The binding of fatty acid observed in three recent Lys49-PLA(2) structures seems to be independent of their quaternary conformation. Cys29 polarization by Lys122 is not significant for BnSP-7 and BnSP-6 or other structures not bound by fatty acids. These structures may be in an "active" state when nothing is bound to them and the Lys122/Cys29 interactions are weak or absent. Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights.,Magro AJ, Soares AM, Giglio JR, Fontes MR Biochem Biophys Res Commun. 2003 Nov 21;311(3):713-20. PMID:14623331[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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