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An Intermolecular π-Stacking Interaction Drives Conformational Changes Necessary to β-Barrel Formation in a Pore-Forming Toxin

The crystal structures of the soluble monomers of the pore-forming cholesterol-dependent cytolysins (CDCs) contain two α-helical bundles that flank a twisted core β-sheet. This protein fold is the hallmark of the CDCs, as well as of the membrane attack complex/perforin immune defense proteins and th...

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Detalles Bibliográficos
Autores principales:	Burns, Joshua R., Morton, Craig J., Parker, Michael W., Tweten, Rodney K.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Society for Microbiology 2019
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6606804/ https://www.ncbi.nlm.nih.gov/pubmed/31266869 http://dx.doi.org/10.1128/mBio.01017-19

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