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4wvm

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Revision as of 09:29, 22 November 2017

Stonustoxin structure

Structural highlights

4wvm is a 2 chain structure with sequence from Synanceia horrida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[STXA_SYNHO] This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.^[1] ^[2] ^[3] [STXB_SYNHO] This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.^[4] ^[5] ^[6]

Publication Abstract from PubMed

The lethal factor in stonefish venom is stonustoxin (SNTX), a heterodimeric cytolytic protein that induces cardiovascular collapse in humans and native predators. Here, using X-ray crystallography, we make the unexpected finding that SNTX is a pore-forming member of an ancient branch of the Membrane Attack Complex-Perforin/Cholesterol-Dependent Cytolysin (MACPF/CDC) superfamily. SNTX comprises two homologous subunits (alpha and beta), each of which comprises an N-terminal pore-forming MACPF/CDC domain, a central focal adhesion-targeting domain, a thioredoxin domain, and a C-terminal tripartite motif family-like PRY SPla and the RYanodine Receptor immune recognition domain. Crucially, the structure reveals that the two MACPF domains are in complex with one another and arranged into a stable early prepore-like assembly. These data provide long sought after near-atomic resolution insights into how MACPF/CDC proteins assemble into prepores on the surface of membranes. Furthermore, our analyses reveal that SNTX-like MACPF/CDCs are distributed throughout eukaryotic life and play a broader, possibly immune-related function outside venom.

Stonefish toxin defines an ancient branch of the perforin-like superfamily.,Ellisdon AM, Reboul CF, Panjikar S, Huynh K, Oellig CA, Winter KL, Dunstone MA, Hodgson WC, Seymour J, Dearden PK, Tweten RK, Whisstock JC, McGowan S Proc Natl Acad Sci U S A. 2015 Dec 1. pii: 201507622. PMID:26627714^[7]

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

References

↑ Poh CH, Yuen R, Khoo HE, Chung M, Gwee M, Gopalakrishnakone P. Purification and partial characterization of stonustoxin (lethal factor) from Synanceja horrida venom. Comp Biochem Physiol B. 1991;99(4):793-8. PMID:1790672
↑ Low KS, Gwee MC, Yuen R, Gopalakrishnakone P, Khoo HE. Stonustoxin: effects on neuromuscular function in vitro and in vivo. Toxicon. 1994 May;32(5):573-81. PMID:8079369
↑ Chen D, Kini RM, Yuen R, Khoo HE. Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues. Biochem J. 1997 Aug 1;325 ( Pt 3):685-91. PMID:9271089
↑ Poh CH, Yuen R, Khoo HE, Chung M, Gwee M, Gopalakrishnakone P. Purification and partial characterization of stonustoxin (lethal factor) from Synanceja horrida venom. Comp Biochem Physiol B. 1991;99(4):793-8. PMID:1790672
↑ Low KS, Gwee MC, Yuen R, Gopalakrishnakone P, Khoo HE. Stonustoxin: effects on neuromuscular function in vitro and in vivo. Toxicon. 1994 May;32(5):573-81. PMID:8079369
↑ Chen D, Kini RM, Yuen R, Khoo HE. Haemolytic activity of stonustoxin from stonefish (Synanceja horrida) venom: pore formation and the role of cationic amino acid residues. Biochem J. 1997 Aug 1;325 ( Pt 3):685-91. PMID:9271089
↑ Ellisdon AM, Reboul CF, Panjikar S, Huynh K, Oellig CA, Winter KL, Dunstone MA, Hodgson WC, Seymour J, Dearden PK, Tweten RK, Whisstock JC, McGowan S. Stonefish toxin defines an ancient branch of the perforin-like superfamily. Proc Natl Acad Sci U S A. 2015 Dec 1. pii: 201507622. PMID:26627714 doi:http://dx.doi.org/10.1073/pnas.1507622112

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wvm"

@@ Line 1: / Line 1: @@
 ==Stonustoxin structure==
 <StructureSection load='4wvm' size='340' side='right' caption='[[4wvm]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4wvm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synanceia_horrida Synanceia horrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WVM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WVM FirstGlance]. <br>
-</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=4wvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wvm OCA], [http://pdbe.org/4wvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wvm RCSB], [http://www.ebi.ac.uk/pdbsum/4wvm PDBsum]</span></td></tr>
+</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=4wvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wvm OCA], [http://pdbe.org/4wvm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wvm RCSB], [http://www.ebi.ac.uk/pdbsum/4wvm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wvm ProSAT]</span></td></tr>
 </table>
 == Function ==

4wvm

From Proteopedia

Revision as of 09:29, 22 November 2017

Stonustoxin structure

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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