Purification, crystallization and characterization of the Pseudomonas outer membrane protein FapF, a functional amyloid transporter.

ABSTRACT: Bacteria often produce extracellular amyloid fibres via a multi-component secretion system. Aggregation-prone, unstructured subunits cross the periplasm and are secreted through the outer membrane, after which they self-assemble. Here, significant progress is presented towards solving the high-resolution crystal structure of the novel amyloid transporter FapF from Pseudomonas, which facilitates the secretion of the amyloid-forming polypeptide FapC across the bacterial outer membrane. This represents the first step towards obtaining structural insight into the products of the Pseudomonas fap operon. Initial attempts at crystallizing full-length and N-terminally truncated constructs by refolding techniques were not successful; however, after preparing FapF^106-430 from the membrane

SUBMITTER: Rouse SL 

PROVIDER: S-EPMC5137466 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature