Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation

ABSTRACT Curli amyloid fibers are produced as part of the extracellular biofilm matrix and are composed primarily of the major structural subunit CsgA. The CsgE chaperone facilitates the secretion of CsgA through CsgG by forming a cap at the base of the nonameric CsgG outer membrane pore. We elucida...

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Detalles Bibliográficos
Autores principales:	Roger D. Klein, Qin Shu, Zachary T. Cusumano, Kanna Nagamatsu, Nathaniel C. Gualberto, Aaron J. L. Lynch, Chao Wu, Wenjie Wang, Neha Jain, Jerome S. Pinkner, Gaya K. Amarasinghe, Scott J. Hultgren, Carl Frieden, Matthew R. Chapman
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2018
Materias:	Escherichia coli functional amyloid nucleation-precipitation bioassembly biofilms curli Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/ff37b00ca12f43a9a3727996214c28c6
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Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation

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