Untangling a Repetitive Amyloid Sequence: Correlating Biofilm‐Derived and Segmentally Labeled Curli Fimbriae by Solid‐State NMR Spectroscopy |
| |
Authors: | Dr Tobias Schubeis Puwei Yuan Dr Mumdooh Ahmed Dr Madhu Nagaraj Dr Barth‐Jan van?Rossum Dr Christiane Ritter |
| |
Institution: | 1. Laboratory of Macromolecular Interactions, Helmholtz‐Zentrum für Infektionsforschung, Inhoffenstrasse 7, 38124 Braunschweig (Germany);2. Department of Physics, Faculty of Science, Suez University, Suez, 43533 (Egypt);3. NMR‐Supported Structural Biology, Leibniz‐Institut für Molekulare Pharmakologie (FMP), Robert‐R?ssle‐Strasse 10, 13125 Berlin (Germany) |
| |
Abstract: | Curli are functional bacterial amyloids produced by an intricate biogenesis machinery. Insights into their folding and regulation can advance our understanding of amyloidogenesis. However, gaining detailed structural information of amyloids, and their tendency for structural polymorphisms, remains challenging. Herein we compare high‐quality solid‐state NMR spectra from biofilm‐derived and recombinantly produced curli and provide evidence that they adopt a similar, well‐defined β‐solenoid arrangement. Curli subunits consist of five sequence repeats, resulting in severe spectral overlap. Using segmental isotope labeling, we obtained the unambiguous sequence‐specific resonance assignments and secondary structure of one repeat, and demonstrate that all repeats are most likely structurally equivalent. |
| |
Keywords: | functional amyloid intein isotopic labeling protein structures solid‐state NMR spectroscopy |
|
|