组氨酸
化学
配体(生物化学)
肽
侧链
淀粉样蛋白(真菌学)
金属
结晶学
蛋白质结构
立体化学
核磁共振波谱
有机化学
氨基酸
生物化学
无机化学
受体
聚合物
作者
Myungwoon Lee,Tuo Wang,Olga V. Makhlynets,Yibing Wu,Nicholas F. Polizzi,Haifan Wu,Pallavi M. Gosavi,Jan Stöhr,Ivan V. Korendovych,William F. DeGrado,Mei Hong
标识
DOI:10.1073/pnas.1706179114
摘要
Significance Functional and pathological amyloid fibrils bind metal ions, but no metal-bound amyloid structures have been determined. Using solid-state NMR and structural bioinformatics, we have determined the oligomeric structure and coordination geometry of a Zn 2+ -mediated amyloid fibril that catalyzes ester hydrolysis. The peptide assembles into parallel β-sheets in which histidines bridge zinc ions to promote β-strand association in a geometry that mediates water activation for catalysis. The study demonstrates an approach for determining the structures of metalloamyloids. The resulting structure defines how metal ions can stabilize amyloids, lends support to the hypothesis that amyloids can serve as well-structured intermediates between amino acids and proteins during the evolution of life, and provides a framework for potential applications in material science.
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