5gaq

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of the Lysenin Pore

5gaq, resolution 3.14Å

Structural highlights

5gaq is a 9 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:	Electron Microscopy, Resolution 3.14Å
Experimental data:	Check to display Experimental Data
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

Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small beta-pore-forming toxins (beta-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive and therefore the mechanism of activation and membrane insertion remains unclear. Here we determine the pore structure of lysenin by single particle cryo-EM, to 3.1 A resolution. The nonameric assembly reveals a long beta-barrel channel spanning the length of the complex that, unexpectedly, includes the two pre-insertion strands flanking the hypothetical membrane-insertion loop. Examination of other members of the aerolysin family reveals high structural preservation in this region, indicating that the membrane-insertion pathway in this family is conserved. For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre-insertion strands, allowing them to form the beta-barrel of the channel.

Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.,Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, Savva CG Nat Commun. 2016 Apr 6;7:11293. doi: 10.1038/ncomms11293. PMID:27048994^[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
↑ Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, Savva CG. Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein. Nat Commun. 2016 Apr 6;7:11293. doi: 10.1038/ncomms11293. PMID:27048994 doi:http://dx.doi.org/10.1038/ncomms11293

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/5gaq"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5gaq is ON HOLD
+==Cryo-EM structure of the Lysenin Pore==
+<SX load='5gaq' size='340' side='right' viewer='molstar' caption='[[5gaq]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5gaq]] is a 9 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=5GAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GAQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.14&#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=5gaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gaq OCA], [https://pdbe.org/5gaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gaq RCSB], [https://www.ebi.ac.uk/pdbsum/5gaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gaq 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 ==
+Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small beta-pore-forming toxins (beta-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive and therefore the mechanism of activation and membrane insertion remains unclear. Here we determine the pore structure of lysenin by single particle cryo-EM, to 3.1 A resolution. The nonameric assembly reveals a long beta-barrel channel spanning the length of the complex that, unexpectedly, includes the two pre-insertion strands flanking the hypothetical membrane-insertion loop. Examination of other members of the aerolysin family reveals high structural preservation in this region, indicating that the membrane-insertion pathway in this family is conserved. For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre-insertion strands, allowing them to form the beta-barrel of the channel.
-Authors: Savva, C.G., Bokori-Brown, M., Martin, T.G., Titball, R.W., Naylor, C.E., Basak, A.K.
+Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.,Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, Savva CG Nat Commun. 2016 Apr 6;7:11293. doi: 10.1038/ncomms11293. PMID:27048994<ref>PMID:27048994</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Basak, A.K]]
+<div class="pdbe-citations 5gaq" style="background-color:#fffaf0;"></div>
-[[Category: Bokori-Brown, M]]
-[[Category: Savva, C.G]]
+==See Also==
-[[Category: Titball, R.W]]
+*[[Cytolysin 3D structures|Cytolysin 3D structures]]
-[[Category: Martin, T.G]]
+== References ==
-[[Category: Naylor, C.E]]
+<references/>
+__TOC__
+</SX>
+[[Category: Eisenia fetida]]
+[[Category: Large Structures]]
+[[Category: Basak AK]]
+[[Category: Bokori-Brown M]]
+[[Category: Martin TG]]
+[[Category: Naylor CE]]
+[[Category: Savva CG]]
+[[Category: Titball RW]]

5gaq

From Proteopedia

Current revision

Cryo-EM structure of the Lysenin Pore

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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