5ec5

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Current revision (06:20, 5 July 2023) (edit) (undo)
 
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<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 ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[5ec5]] is a 18 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=5EC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EC5 FirstGlance]. <br>
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</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>
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</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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ec5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ec5 OCA], [https://pdbe.org/5ec5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ec5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ec5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ec5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eisfe]]
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[[Category: Eisenia fetida]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Anderluh, G]]
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[[Category: Anderluh G]]
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[[Category: Bruce, M]]
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[[Category: Bruce M]]
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[[Category: Jayasinghe, L]]
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[[Category: Jayasinghe L]]
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[[Category: Kisovec, M]]
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[[Category: Kisovec M]]
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[[Category: Podobnik, M]]
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[[Category: Podobnik M]]
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[[Category: Rojko, N]]
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[[Category: Rojko N]]
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[[Category: Savory, P]]
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[[Category: Savory P]]
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[[Category: Functional pore]]
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[[Category: Invertebrate cytolysin]]
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[[Category: Nanopore]]
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[[Category: Nonamer]]
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[[Category: Toxin]]
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Current revision

Crystal structure of lysenin pore

PDB ID 5ec5

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