6myk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Pleurotus ostreatus OstreolysinA mutant E69A with Bis-Tris== | |
| + | <StructureSection load='6myk' size='340' side='right' caption='[[6myk]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6myk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MYK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6myk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6myk OCA], [http://pdbe.org/6myk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6myk RCSB], [http://www.ebi.ac.uk/pdbsum/6myk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6myk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:30712872</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6myk" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Endapally, S]] | [[Category: Endapally, S]] | ||
| + | [[Category: Radhakrishnan, A]] | ||
| + | [[Category: Tomchick, D R]] | ||
| + | [[Category: Beta-sandwich fold]] | ||
| + | [[Category: Membrane binding protein]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 09:36, 13 February 2019
Pleurotus ostreatus OstreolysinA mutant E69A with Bis-Tris
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