Untangling a Repetitive Amyloid Sequence: Correlating Biofilm-Derived and Segmentally Labeled Curli Fimbriae by Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl
; 54(49): 14669-72, 2015 Dec 01.
Article
in En
| MEDLINE
| ID: mdl-26474178
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 ß-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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Fimbriae, Bacterial
/
Biofilms
/
Amyloid
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2015
Document type:
Article