4wvm: Difference between revisions

Latest revision as of 00:55, 28 December 2023

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.
Method:	X-ray diffraction, Resolution 3.1Å
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]

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^[4]

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
↑ 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:https://dx.doi.org/10.1073/pnas.1507622112

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OCA

[1] 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

[2] 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

[3] 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

[4] 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:https://dx.doi.org/10.1073/pnas.1507622112

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
 ==Stonustoxin structure==
-<StructureSection load='4wvm' size='340' side='right' caption='[[4wvm]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<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>
+<table><tr><td colspan='2'>[[4wvm]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wvm 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]] 3.1&#8491;</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=4wvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wvm OCA], [https://pdbe.org/4wvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wvm RCSB], [https://www.ebi.ac.uk/pdbsum/4wvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wvm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/STXA_SYNHO 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.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref>  [[http://www.uniprot.org/uniprot/STXB_SYNHO 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.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref>
+[https://www.uniprot.org/uniprot/STXA_SYNHO 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.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 4wvm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytolysin 3D structures|Cytolysin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Synanceia horrida]]
-[[Category: Ellisdon, A M]]
+[[Category: Ellisdon AM]]
-[[Category: McGowan, S]]
+[[Category: McGowan S]]
-[[Category: Panjikar, S]]
+[[Category: Panjikar S]]
-[[Category: Whisstock, J C]]
+[[Category: Whisstock JC]]
-[[Category: Cytolysin]]
-[[Category: Macpf cdc]]
-[[Category: Membrane attack complex]]
-[[Category: Perforin cholesterol dependent]]
-[[Category: Pry]]
-[[Category: Spry]]
-[[Category: Thioredoxin focal adhesion targeting]]
-[[Category: Toxin]]
-[[Category: Venom]]

4wvm: Difference between revisions

Latest revision as of 00:55, 28 December 2023

Stonustoxin structure

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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