Cryo-EM structure of a catalytic amyloid fibril

被引:6
|
作者
Heerde, Thomas [1 ]
Bansal, Akanksha [1 ]
Schmidt, Matthias [1 ]
Faendrich, Marcus [1 ]
机构
[1] Ulm Univ, Inst Prot Biochem, D-89081 Ulm, Germany
来源
SCIENTIFIC REPORTS | 2023年 / 13卷 / 01期
关键词
BINDING SITES; DISEASE; HYDROLYSIS; STABILITY; PROVIDES;
D O I
10.1038/s41598-023-30711-y
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction. In this study we used cryo-electron microcopy to analyze the amyloid fibril structure and the catalytic center of amyloid fibrils that hydrolyze ester bonds. Our findings show that catalytic amyloid fibrils are polymorphic and consist of similarly structured, zipper-like building blocks that consist of mated cross-beta sheets. These building blocks define the fibril core, which is decorated by a peripheral leaflet of peptide molecules. The observed structural arrangement differs from previously described catalytic amyloid fibrils and yielded a new model of the catalytic center.
引用
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页数:8
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