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Publication Abstract from PubMed

Curli are functional amyloids that form a major part of the biofilm produced by many enterobacteriaceae. A multi protein system around the outer membrane protein CsgG is in charge of the export and controlled propagation of the main Curli subunits, CsgA and CsgB. CsgF is essential for the linkage of the main amyloid-forming proteins to the cell surface. Here, we present a profound biochemical and biophysical characterization of recombinant CsgF, highlighted by a solution NMR structure of CsgF in the presence of DHPC micelles. Interestingly, CsgF contains large unstructured domains and does not show a globular fold. The data presented sheds new light on the molecular mechanism of Curli amyloid surface attachment. This article is protected by copyright. All rights reserved.

Structural and functional characterization of the Curli adaptor protein CsgF.,Schubeis T, Spehr J, Viereck J, Kopping L, Nagaraj M, Ahmed M, Ritter C FEBS Lett. 2018 Feb 10. doi: 10.1002/1873-3468.13002. PMID:29427517^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.