5ec5

From Proteopedia

(Difference between revisions)

Revision as of 06:52, 22 April 2020

Crystal structure of lysenin pore

Structural highlights

5ec5 is a 18 chain structure with sequence from Eisfe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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

The invertebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes many representatives from pathogenic bacteria. Here we report the crystal structure of the lysenin pore and provide insights into its assembly mechanism. The lysenin pore is assembled from nine monomers via dramatic reorganization of almost half of the monomeric subunit structure leading to a beta-barrel pore approximately 10 nm long and 1.6-2.5 nm wide. The lysenin pore is devoid of additional luminal compartments as commonly found in other toxin pores. Mutagenic analysis and atomic force microscopy imaging, together with these structural insights, suggest a mechanism for pore assembly for lysenin. These insights are relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria.

Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.,Podobnik M, Savory P, Rojko N, Kisovec M, Wood N, Hambley R, Pugh J, Wallace EJ, McNeill L, Bruce M, Liko I, Allison TM, Mehmood S, Yilmaz N, Kobayashi T, Gilbert RJ, Robinson CV, Jayasinghe L, Anderluh G Nat Commun. 2016 May 12;7:11598. doi: 10.1038/ncomms11598. PMID:27176125^[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
↑ Podobnik M, Savory P, Rojko N, Kisovec M, Wood N, Hambley R, Pugh J, Wallace EJ, McNeill L, Bruce M, Liko I, Allison TM, Mehmood S, Yilmaz N, Kobayashi T, Gilbert RJ, Robinson CV, Jayasinghe L, Anderluh G. Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly. Nat Commun. 2016 May 12;7:11598. doi: 10.1038/ncomms11598. PMID:27176125 doi:http://dx.doi.org/10.1038/ncomms11598

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/5ec5"

@@ Line 1: / Line 1: @@
 ==Crystal structure of lysenin pore==
-<StructureSection load='5ec5' size='340' side='right' caption='[[5ec5]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='5ec5' size='340' side='right'caption='[[5ec5]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ec5]] is a 18 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EC5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ec5]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Eisfe Eisfe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EC5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EC5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MBO:MERCURIBENZOIC+ACID'>MBO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MBO:MERCURIBENZOIC+ACID'>MBO</scene></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=5ec5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ec5 OCA], [http://pdbe.org/5ec5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ec5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ec5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ec5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ec5 OCA], [http://pdbe.org/5ec5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ec5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ec5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ec5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 5ec5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytolysin 3D structures|Cytolysin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Eisfe]]
+[[Category: Large Structures]]
 [[Category: Anderluh, G]]
 [[Category: Bruce, M]]

5ec5

From Proteopedia

Revision as of 06:52, 22 April 2020

Crystal structure of 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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