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pneumolysin, domain, article, structure, membrane, residues, google, scholar, toxin, cas, binding, prepore, activity, crystal, fig, pore, mutations, interface, monomers, nature, fluorescence, packing, data, structures, domains, formation, arg, cell, protein, hemolytic, form, wildtype, mutants, membranebinding, surface, complex, contacts, interactions, molecular, pneumoniae, loop, adjacent, argala, gluala, streptococcus, cells, intermolecular, cdc, tryptophanrich, table,

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nature portfolio privacy policy high-resolution x-ray structures model-building tools advertising nature 0/ reprints middle c-terminal membrane-binding domain n-terminal his6 tag comprehensive python-based system large beta-barrel pore7 high-resolution data means human acute-phase protein extended beta-hairpins penetrating tryptophan-rich flips outwards social media otitis media bacterial cholesterol-dependent cytolysin chilled phosphate-buffered saline stable protein-protein complexes23 membrane-surface bound pre-pore maltose-binding protein fusion ring-shaped pre-pore pore-forming toxins putative membrane-binding conformation thermo scientific permissions membrane-spanning β-hairpins pre-pore complex jamie access mutant toxins bind monomer/monomer interface leads putative carbohydrate-binding residues cholesterol-dependent cytolysins pneumolysin red blood cells pore-forming protein toxin protein crystallography reveals molecular details full-length pneumolysin structure full size image wild-type toxin lead double mutant glu434ala + tyr461ala privacy glu434ala + arg437ala double mutant host cells involving pore-forming toxin intermedilysin threonine-leucine pair phosphate-buffered saline competing financial interests

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         headline:The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex
         description:Pneumolysin is a cholesterol-dependent cytolysin (CDC) and virulence factor of Streptococcus pneumoniae. It kills cells by forming pores assembled from oligomeric rings in cholesterol-containing membranes. Cryo-EM has revealed the structures of the membrane-surface bound pre-pore and inserted-pore oligomers, however the molecular contacts that mediate these oligomers are unknown because high-resolution information is not available. Here we have determined the crystal structure of full-length pneumolysin at 1.98 Å resolution. In the structure, crystal contacts demonstrate the likely interactions that enable polymerisation on the cell membrane and the molecular packing of the pre-pore complex. The hemolytic activity is abrogated in mutants that disrupt these intermolecular contacts, highlighting their importance during pore formation. An additional crystal structure of the membrane-binding domain alone suggests that changes in the conformation of a tryptophan rich-loop at the base of the toxin promote monomer-monomer interactions upon membrane binding by creating new contacts. Notably, residues at the interface are conserved in other members of the CDC family, suggesting a common mechanism for pore and pre-pore assembly.
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      headline:The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex
      description:Pneumolysin is a cholesterol-dependent cytolysin (CDC) and virulence factor of Streptococcus pneumoniae. It kills cells by forming pores assembled from oligomeric rings in cholesterol-containing membranes. Cryo-EM has revealed the structures of the membrane-surface bound pre-pore and inserted-pore oligomers, however the molecular contacts that mediate these oligomers are unknown because high-resolution information is not available. Here we have determined the crystal structure of full-length pneumolysin at 1.98 Å resolution. In the structure, crystal contacts demonstrate the likely interactions that enable polymerisation on the cell membrane and the molecular packing of the pre-pore complex. The hemolytic activity is abrogated in mutants that disrupt these intermolecular contacts, highlighting their importance during pore formation. An additional crystal structure of the membrane-binding domain alone suggests that changes in the conformation of a tryptophan rich-loop at the base of the toxin promote monomer-monomer interactions upon membrane binding by creating new contacts. Notably, residues at the interface are conserved in other members of the CDC family, suggesting a common mechanism for pore and pre-pore assembly.
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