Laboratory of Macromolecular Interactions, Helmholtz-Zentrum für Infektionsforschung, Inhoffenstrasse 7, 38124 Braunschweig (Germany).
Department of Physics, Faculty of Science, Suez University, Suez, 43533 (Egypt).
Angew Chem Int Ed Engl. 2015 Dec 1;54(49):14669-72. doi: 10.1002/anie.201506772. Epub 2015 Oct 16.
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.
卷曲菌是由复杂的生物发生机制产生的功能性细菌淀粉样蛋白。深入了解它们的折叠和调节可以促进我们对淀粉样蛋白形成的理解。然而，获得淀粉样蛋白的详细结构信息及其结构多态性的倾向仍然具有挑战性。在此，我们比较了生物膜衍生和重组产生的卷曲菌的高质量固态 NMR 谱，并提供了它们采用相似的、明确的β-发夹排列的证据。卷曲菌亚基由五个序列重复组成，导致光谱严重重叠。通过分段同位素标记，我们获得了一个重复的明确的序列特异性共振分配和二级结构，并证明所有重复很可能在结构上是等效的。
