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| | <StructureSection load='6myj' size='340' side='right'caption='[[6myj]], [[Resolution|resolution]] 1.33Å' scene=''> | | <StructureSection load='6myj' size='340' side='right'caption='[[6myj]], [[Resolution|resolution]] 1.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6myj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Oyster_mushroom Oyster mushroom]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MYJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6myj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_ostreatus Pleurotus ostreatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MYJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K6V:N-[(2S)-1-hydroxypropan-2-yl]butanamide'>K6V</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.33Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OlyA6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5322 Oyster mushroom])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K6V:N-[(2S)-1-hydroxypropan-2-yl]butanamide'>K6V</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6myj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6myj OCA], [http://pdbe.org/6myj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6myj RCSB], [http://www.ebi.ac.uk/pdbsum/6myj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6myj ProSAT]</span></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=6myj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6myj OCA], [https://pdbe.org/6myj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6myj RCSB], [https://www.ebi.ac.uk/pdbsum/6myj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6myj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OLYA6_PLEOS OLYA6_PLEOS]] Has hemolytic activity against bovine erythrocytes at nanomolar concentrations in vitro. Promotes active pleurotolysin B (PlyB)-dependent permeabilization of membranes rich in cholesterol and sphingomyelin. May play an important role in the initial phase of fungal fruiting.<ref>PMID:12020804</ref> <ref>PMID:23806422</ref> | + | [https://www.uniprot.org/uniprot/OLYA6_PLEOS OLYA6_PLEOS] Has hemolytic activity against bovine erythrocytes at nanomolar concentrations in vitro. Promotes active pleurotolysin B (PlyB)-dependent permeabilization of membranes rich in cholesterol and sphingomyelin. May play an important role in the initial phase of fungal fruiting.<ref>PMID:12020804</ref> <ref>PMID:23806422</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oyster mushroom]] | + | [[Category: Pleurotus ostreatus]] |
| - | [[Category: Endapally, S]] | + | [[Category: Endapally S]] |
| - | [[Category: Radhakrishnan, A]] | + | [[Category: Radhakrishnan A]] |
| - | [[Category: Tomchick, D R]] | + | [[Category: Tomchick DR]] |
| - | [[Category: Beta-sandwich fold]]
| + | |
| - | [[Category: Membrane binding protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| Structural highlights
Function
OLYA6_PLEOS Has hemolytic activity against bovine erythrocytes at nanomolar concentrations in vitro. Promotes active pleurotolysin B (PlyB)-dependent permeabilization of membranes rich in cholesterol and sphingomyelin. May play an important role in the initial phase of fungal fruiting.[1] [2]
Publication Abstract from PubMed
Sphingomyelin and cholesterol are essential lipids that are enriched in plasma membranes of animal cells, where they interact to regulate membrane properties and many intracellular signaling processes. Despite intense study, the interaction between these lipids in membranes is not well understood. Here, structural and biochemical analyses of ostreolysin A (OlyA), a protein that binds to membranes only when they contain both sphingomyelin and cholesterol, reveal that sphingomyelin adopts two distinct conformations in membranes when cholesterol is present. One conformation, bound by OlyA, is induced by stoichiometric, exothermic interactions with cholesterol, properties that are consistent with sphingomyelin/cholesterol complexes. In its second conformation, sphingomyelin is free from cholesterol and does not bind OlyA. A point mutation abolishes OlyA's ability to discriminate between these two conformations. In cells, levels of sphingomyelin/cholesterol complexes are held constant over a wide range of plasma membrane cholesterol concentrations, enabling precise regulation of the chemical activity of cholesterol.
Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes.,Endapally S, Frias D, Grzemska M, Gay A, Tomchick DR, Radhakrishnan A Cell. 2019 Jan 25. pii: S0092-8674(18)31656-8. doi: 10.1016/j.cell.2018.12.042. PMID:30712872[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Berne S, Krizaj I, Pohleven F, Turk T, Macek P, Sepcic K. Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting. Biochim Biophys Acta. 2002 Apr 15;1570(3):153-9. PMID:12020804
- ↑ Ota K, Leonardi A, Mikelj M, Skocaj M, Wohlschlager T, Kunzler M, Aebi M, Narat M, Krizaj I, Anderluh G, Sepcic K, Macek P. Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B. Biochimie. 2013 Oct;95(10):1855-64. doi: 10.1016/j.biochi.2013.06.012. Epub 2013 , Jun 25. PMID:23806422 doi:http://dx.doi.org/10.1016/j.biochi.2013.06.012
- ↑ Endapally S, Frias D, Grzemska M, Gay A, Tomchick DR, Radhakrishnan A. Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes. Cell. 2019 Jan 25. pii: S0092-8674(18)31656-8. doi: 10.1016/j.cell.2018.12.042. PMID:30712872 doi:http://dx.doi.org/10.1016/j.cell.2018.12.042
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