1pc9

From Proteopedia

(Difference between revisions)

Revision as of 08:01, 15 February 2018

Crystal Structure of BnSP-6, a Lys49-Phospholipase A2

Structural highlights

1pc9 is a 2 chain structure with sequence from Bothrops neuwiedi pauloensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1pa0
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[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 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^[4]

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

References

↑ Soares AM, Guerra-Sa R, Borja-Oliveira CR, Rodrigues VM, Rodrigues-Simioni L, Rodrigues V, Fontes MR, Lomonte B, Gutierrez JM, Giglio JR. Structural and functional characterization of BnSP-7, a Lys49 myotoxic phospholipase A(2) homologue from Bothrops neuwiedi pauloensis venom. Arch Biochem Biophys. 2000 Jun 15;378(2):201-9. PMID:10860537 doi:http://dx.doi.org/10.1006/abbi.2000.1790
↑ Rodrigues VM, Soares AM, Mancin AC, Fontes MR, Homsi-Brandeburgo MI, Giglio JR. Geographic variations in the composition of myotoxins from Bothrops neuwiedi snake venoms: biochemical characterization and biological activity. Comp Biochem Physiol A Mol Integr Physiol. 1998 Nov;121(3):215-22. PMID:9972319
↑ Magro AJ, Soares AM, Giglio JR, Fontes MR. Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights. Biochem Biophys Res Commun. 2003 Nov 21;311(3):713-20. PMID:14623331
↑ Magro AJ, Soares AM, Giglio JR, Fontes MR. Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A(2): quaternary structure and inhibition mechanism insights. Biochem Biophys Res Commun. 2003 Nov 21;311(3):713-20. PMID:14623331

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pc9"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of BnSP-6, a Lys49-Phospholipase A2==
 <StructureSection load='1pc9' size='340' side='right' caption='[[1pc9]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pa0|1pa0]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pc9 OCA], [http://pdbe.org/1pc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1pc9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pc9 OCA], [http://pdbe.org/1pc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1pc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pc9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pc9_consurf.spt"</scriptWhenChecked>
+    <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/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1pc9

From Proteopedia

Revision as of 08:01, 15 February 2018

Crystal Structure of BnSP-6, a Lys49-Phospholipase A2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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