This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1o71

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 18:18, 20 November 2019

Crystal structure of the water-soluble state of the pore-forming cytolysin Sticholysin II complexed with glycerol

Structural highlights

1o71 is a 2 chain structure with sequence from Stoichactis helianthus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1gwy, 1o72
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTP2_STIHL] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.^[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

Sticholysin II (StnII) is a pore-forming protein (PFP) produced by the sea anemone Stichodactyla helianthus. We found out that StnII exists in a monomeric soluble state but forms tetramers in the presence of a lipidic interface. Both structures have been independently determined at 1.7 A and 18 A resolution, respectively, by using X-ray crystallography and electron microscopy of two-dimensional crystals. Besides, the structure of soluble StnII complexed with phosphocholine, determined at 2.4 A resolution, reveals a phospholipid headgroup binding site, which is located in a region with an unusually high abundance of aromatic residues. Fitting of the atomic model into the electron microscopy density envelope suggests that while the beta sandwich structure of the protein remains intact upon oligomerization, the N-terminal region and a flexible and highly basic loop undergo significant conformational changes. These results provide the structural basis for the membrane recognition step of actinoporins and unexpected insights into the oligomerization step.

Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation.,Mancheno JM, Martin-Benito J, Martinez-Ripoll M, Gavilanes JG, Hermoso JA Structure. 2003 Nov;11(11):1319-28. PMID:14604522^[3]

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

References

↑ Lanio ME, Morera V, Alvarez C, Tejuca M, Gomez T, Pazos F, Besada V, Martinez D, Huerta V, Padron G, de los Angeles Chavez M. Purification and characterization of two hemolysins from Stichodactyla helianthus. Toxicon. 2001 Feb-Mar;39(2-3):187-94. PMID:10978735
↑ Martinez D, Campos AM, Pazos F, Alvarez C, Lanio ME, Casallanovo F, Schreier S, Salinas RK, Vergara C, Lissi E. Properties of St I and St II, two isotoxins isolated from Stichodactyla helianthus: a comparison. Toxicon. 2001 Oct;39(10):1547-60. PMID:11478962
↑ Mancheno JM, Martin-Benito J, Martinez-Ripoll M, Gavilanes JG, Hermoso JA. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure. 2003 Nov;11(11):1319-28. PMID:14604522

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/1o71"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the water-soluble state of the pore-forming cytolysin Sticholysin II complexed with glycerol==
-<StructureSection load='1o71' size='340' side='right' caption='[[1o71]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
+<StructureSection load='1o71' size='340' side='right'caption='[[1o71]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1o71]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Stoichactis_helianthus Stoichactis helianthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O71 FirstGlance]. <br>
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 1o71" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytolysin 3D structures|Cytolysin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Stoichactis helianthus]]
 [[Category: Gavilanes, J G]]

1o71

From Proteopedia

Revision as of 18:18, 20 November 2019

Crystal structure of the water-soluble state of the pore-forming cytolysin Sticholysin II complexed with glycerol

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox