3zxg

From Proteopedia

(Difference between revisions)

Current revision

lysenin sphingomyelin complex

Structural highlights

3zxg is a 2 chain structure with sequence from Eisenia fetida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.12Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TXL_EISFE Pore-forming toxin that specifically binds sphingomyelin in the plasma membrane of various cells. Has hemolytic activity. Is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10 times more effective than lysenin-related protein 1.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Pore-forming proteins insert from solution into membranes to create lesions, undergoing a structural rearrangement often accompanied by oligomerization. Lysenin, a pore-forming toxin from the earthworm Eisenia fetida, specifically interacts with sphingomyelin (SM) and may confer innate immunity against parasites by attacking their membranes to form pores. SM has important roles in cell membranes and lysenin is a popular SM-labeling reagent. The structure of lysenin suggests common ancestry with other pore-forming proteins from a diverse set of eukaryotes and prokaryotes. The complex with SM shows the mode of its recognition by a protein in which both the phosphocholine headgroup and one acyl tail are specifically bound. Lipid interaction studies and assays using viable target cells confirm the functional reliance of lysenin on this form of SM recognition.

Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.,De Colibus L, Sonnen AF, Morris KJ, Siebert CA, Abrusci P, Plitzko J, Hodnik V, Leippe M, Volpi E, Anderluh G, Gilbert RJ Structure. 2012 Sep 5;20(9):1498-507. Epub 2012 Jul 19. PMID:22819216^[7]

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

References

↑ Kobayashi H, Sekizawa Y, Aizu M, Umeda M. Lethal and non-lethal responses of spermatozoa from a wide variety of vertebrates and invertebrates to lysenin, a protein from the coelomic fluid of the earthworm Eisenia foetida. J Exp Zool. 2000 Apr 1;286(5):538-49. PMID:10684578
↑ Yamaji-Hasegawa A, Makino A, Baba T, Senoh Y, Kimura-Suda H, Sato SB, Terada N, Ohno S, Kiyokawa E, Umeda M, Kobayashi T. Oligomerization and pore formation of a sphingomyelin-specific toxin, lysenin. J Biol Chem. 2003 Jun 20;278(25):22762-70. Epub 2003 Apr 3. PMID:12676961 doi:http://dx.doi.org/10.1074/jbc.M213209200
↑ Kiyokawa E, Makino A, Ishii K, Otsuka N, Yamaji-Hasegawa A, Kobayashi T. Recognition of sphingomyelin by lysenin and lysenin-related proteins. Biochemistry. 2004 Aug 3;43(30):9766-73. PMID:15274631 doi:http://dx.doi.org/10.1021/bi049561j
↑ Kobayashi H, Suzuki H, Ohta N. Exfoliation of the epidermal cells and defecation by amphibian larvae in response to coelomic fluid and lysenin from the earthworm Eisenia foetida. Biomed Res. 2006 Aug;27(4):169-81. PMID:16971770
↑ Sekizawa Y, Kubo T, Kobayashi H, Nakajima T, Natori S. Molecular cloning of cDNA for lysenin, a novel protein in the earthworm Eisenia foetida that causes contraction of rat vascular smooth muscle. Gene. 1997 May 20;191(1):97-102. PMID:9210594
↑ Yamaji A, Sekizawa Y, Emoto K, Sakuraba H, Inoue K, Kobayashi H, Umeda M. Lysenin, a novel sphingomyelin-specific binding protein. J Biol Chem. 1998 Feb 27;273(9):5300-6. PMID:9478988
↑ De Colibus L, Sonnen AF, Morris KJ, Siebert CA, Abrusci P, Plitzko J, Hodnik V, Leippe M, Volpi E, Anderluh G, Gilbert RJ. Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition. Structure. 2012 Sep 5;20(9):1498-507. Epub 2012 Jul 19. PMID:22819216 doi:http://dx.doi.org/10.1016/j.str.2012.06.011

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zxg"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3zxg is ON HOLD
+==lysenin sphingomyelin complex==
+<StructureSection load='3zxg' size='340' side='right'caption='[[3zxg]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3zxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZXG 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]] 3.12&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0SM:TRIMETHYL-[2-[[(2S,3S)-2-(OCTADECANOYLAMINO)-3-OXIDANYL-BUTOXY]-OXIDANYL-PHOSPHORYL]OXYETHYL]AZANIUM'>0SM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3zxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zxg OCA], [https://pdbe.org/3zxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zxg RCSB], [https://www.ebi.ac.uk/pdbsum/3zxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zxg ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TXL_EISFE TXL_EISFE] Pore-forming toxin that specifically binds sphingomyelin in the plasma membrane of various cells. Has hemolytic activity. Is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10 times more effective than lysenin-related protein 1.<ref>PMID:10684578</ref> <ref>PMID:12676961</ref> <ref>PMID:15274631</ref> <ref>PMID:16971770</ref> <ref>PMID:9210594</ref> <ref>PMID:9478988</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Pore-forming proteins insert from solution into membranes to create lesions, undergoing a structural rearrangement often accompanied by oligomerization. Lysenin, a pore-forming toxin from the earthworm Eisenia fetida, specifically interacts with sphingomyelin (SM) and may confer innate immunity against parasites by attacking their membranes to form pores. SM has important roles in cell membranes and lysenin is a popular SM-labeling reagent. The structure of lysenin suggests common ancestry with other pore-forming proteins from a diverse set of eukaryotes and prokaryotes. The complex with SM shows the mode of its recognition by a protein in which both the phosphocholine headgroup and one acyl tail are specifically bound. Lipid interaction studies and assays using viable target cells confirm the functional reliance of lysenin on this form of SM recognition.
-Authors: De Colibus, L., Sonnen, A.F.P., Morris, K.J., Siebert, C.A., Abrusci, P., Plitzko, J., Hodnik, V., Leippe, M., Volpi, E., Anderluh, G., Gilbert, R.J.C.
+Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition.,De Colibus L, Sonnen AF, Morris KJ, Siebert CA, Abrusci P, Plitzko J, Hodnik V, Leippe M, Volpi E, Anderluh G, Gilbert RJ Structure. 2012 Sep 5;20(9):1498-507. Epub 2012 Jul 19. PMID:22819216<ref>PMID:22819216</ref>
-Description: lysenin sphingomyelin complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3zxg" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytolysin 3D structures|Cytolysin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Eisenia fetida]]
+[[Category: Large Structures]]
+[[Category: Abrusci P]]
+[[Category: Anderluh G]]
+[[Category: De Colibus L]]
+[[Category: Gilbert RJC]]
+[[Category: Hodnik V]]
+[[Category: Leippe M]]
+[[Category: Morris KJ]]
+[[Category: Plitzko J]]
+[[Category: Siebert CA]]
+[[Category: Sonnen AFP]]
+[[Category: Volpi E]]

3zxg

From Proteopedia

Current revision

lysenin sphingomyelin complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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