We are analyzing https://link.springer.com/article/10.1007/s13238-010-0012-3.

Title:
Crystal structure of cytotoxin protein suilysin from Streptococcus suis | Protein & Cell
Description:
Cholesterol-dependent cytolysins (CDC) are pore forming toxins. A prototype of the CDC family members is perfringolysin O (PFO), which directly binds to the cell membrane enriched in cholesterol, causing cell lysis. However, an exception of this general observation is intermedilysin (ILY) of Streptococcus intermedius, which requires human CD59 as a receptor in addition to cholesterol for its hemolytic activity. A possible explanation of this functional difference is the conformational variation between the C-terminal domains of the two toxins, particularly in the highly conserved undecapeptide termed tryptophan rich motif. Here, we present the crystal structure of suilysin, a CDC toxin from the infectious swine pathogen Streptococcus suis. Like PFO, suilysin does not require a host receptor for hemolytic activity; yet the crystal structure of suilysin exhibits a similar conformation in the tryptophan rich motif to ILY. This observation suggests that the current view of the structure-function relationship between CDC proteins and membrane association is far from complete.
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Keywords {🔍}

article, pubmed, google, scholar, cas, cholesteroldependent, protein, structure, biol, tweten, crystallogr, central, cytolysins, cell, suilysin, streptococcus, membrane, cytolysin, johnson, crystal, acta, mol, parker, privacy, cookies, research, suis, toxins, intermedilysin, proteins, structural, bacterial, content, data, information, publish, search, download, cdc, pore, human, rossjohn, analysis, journal, cytotoxin, huang, huamao, zhang, jianguo, xuemei,

Topics {✒️}

versatile pore-forming toxins intersubunit beta-strand alignment beta-sheet transition identified specific protein-protein interfaces bacterial toxin pneumolysin cholesterol-dependent cytolysin secreted thiol-activated cytolysin tryptophan rich motif pore forming toxins pore-forming toxins cholesterol-sensitive membrane interactions cholesterol-dependent cytolysin intermedilysin specific protein-membrane contacts related subjects x-ray structure cdc proteins cholesterol-dependent cytolysins cholesterol-dependent cytolysin protein structure analysis privacy choices/manage cookies bacterial attack water-soluble state causing cell lysis cell membrane enriched authors contributed equally article xu proteins cytotoxin protein suilysin huamao du main content log membrane-dependent conformational xuemei li human cells secreted protein cell 1 structure-function relationship european economic area c-terminal domains negative intensity observations van den berg clustal_x windows interface infectious disease prevention human liver abscess protein structure conditions privacy policy search search crystal structure acta crystallographica d50 acta cryst a34 requires human cd59 quality analysis tools

Schema {🗺️}

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         headline:Crystal structure of cytotoxin protein suilysin from Streptococcus suis
         description:Cholesterol-dependent cytolysins (CDC) are pore forming toxins. A prototype of the CDC family members is perfringolysin O (PFO), which directly binds to the cell membrane enriched in cholesterol, causing cell lysis. However, an exception of this general observation is intermedilysin (ILY) of Streptococcus intermedius, which requires human CD59 as a receptor in addition to cholesterol for its hemolytic activity. A possible explanation of this functional difference is the conformational variation between the C-terminal domains of the two toxins, particularly in the highly conserved undecapeptide termed tryptophan rich motif. Here, we present the crystal structure of suilysin, a CDC toxin from the infectious swine pathogen Streptococcus suis. Like PFO, suilysin does not require a host receptor for hemolytic activity; yet the crystal structure of suilysin exhibits a similar conformation in the tryptophan rich motif to ILY. This observation suggests that the current view of the structure-function relationship between CDC proteins and membrane association is far from complete.
         datePublished:2010-02-07T00:00:00Z
         dateModified:2010-02-07T00:00:00Z
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            cholesterol-dependent cytolysin
            crystal structure
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ScholarlyArticle:
      headline:Crystal structure of cytotoxin protein suilysin from Streptococcus suis
      description:Cholesterol-dependent cytolysins (CDC) are pore forming toxins. A prototype of the CDC family members is perfringolysin O (PFO), which directly binds to the cell membrane enriched in cholesterol, causing cell lysis. However, an exception of this general observation is intermedilysin (ILY) of Streptococcus intermedius, which requires human CD59 as a receptor in addition to cholesterol for its hemolytic activity. A possible explanation of this functional difference is the conformational variation between the C-terminal domains of the two toxins, particularly in the highly conserved undecapeptide termed tryptophan rich motif. Here, we present the crystal structure of suilysin, a CDC toxin from the infectious swine pathogen Streptococcus suis. Like PFO, suilysin does not require a host receptor for hemolytic activity; yet the crystal structure of suilysin exhibits a similar conformation in the tryptophan rich motif to ILY. This observation suggests that the current view of the structure-function relationship between CDC proteins and membrane association is far from complete.
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         suilysin
         cholesterol-dependent cytolysin
         crystal structure
         Biochemistry
         general
         Protein Science
         Cell Biology
         Stem Cells
         Human Genetics
         Developmental Biology
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            type:Organization
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      affiliation:
            name:Chinese Academy of Sciences
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      name:State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Communicable Disease Control and Prevention, Beijing, China
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      name:National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
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