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

ABSTRACT 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 protei...

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Bibliographic Details
Main Authors: Joshua R. Burns, Craig J. Morton, Michael W. Parker, Rodney K. Tweten
Format: article
Language:EN
Published: American Society for Microbiology 2019
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Online Access:https://doaj.org/article/70c7a6f486474d4393e2f0732710f0ed
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