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DOI	10.1073/pnas.1706179114
	Zinc-binding structure of a catalytic amyloid from solid-state NMR
	Lee M.; Wang T.; Makhlynets O.V.; Wu Y.; Polizzi N.F.; Wu H.; Gosavi P.M.; Stöhr J.; Korendovych I.V.; Degrado W.F.; Hong M.
发表日期	2017
ISSN	0027-8424
起始页码	6191
结束页码	6196
卷号	114 期号:24
英文摘要	Throughout biology, amyloids are key structures in both functional proteins and the end product of pathologic protein misfolding. Amyloids might also represent an early precursor in the evolution of life because of their small molecular size and their ability to selfpurify and catalyze chemical reactions. They also provide attractive backbones for advanced materials. When β-strands of an amyloid are arranged parallel and in register, side chains from the same position of each chain align, facilitating metal chelation when the residues are good ligands such as histidine. High-resolution structures of metalloamyloids are needed to understand the molecular bases of metal-amyloid interactions. Here we combine solid-state NMR and structural bioinformatics to determine the structure of a zinc-bound metalloamyloid that catalyzes ester hydrolysis. The peptide forms amphiphilic parallel β-sheets that assemble into stacked bilayers with alternating hydrophobic and polar interfaces. The hydrophobic interface is stabilized by apolar side chains from adjacent sheets, whereas the hydrated polar interface houses the Zn2+-binding histidines with binding geometries unusual in proteins. Each Zn2+ has two bis-coordinated histidine ligands, which bridge adjacent strands to form an infinite metal-ligand chain along the fibril axis. A third histidine completes the protein ligand environment, leaving a free site on the Zn2+ for water activation. This structure defines a class of materials, which we call metal-peptide frameworks. The structure reveals a delicate interplay through which metal ions stabilize the amyloid structure, which in turn shapes the ligand geometry and catalytic reactivity of Zn2+.
英文关键词	Histidine; Magic angle spinning; Metal-peptide framework; Metalloprotein
语种	英语
scopus关键词	amphophile; amyloid protein; histidine; ligand; zinc; zinc binding protein; amyloid; metalloprotein; water; Article; beta sheet; binding site; catalyst; hydrophobicity; nuclear magnetic resonance; priority journal; protein hydrolysis; protein structure; proton nuclear magnetic resonance; reversed phase high performance liquid chromatography; solid phase synthesis; solid state; structural bioinformatics; transmission electron microscopy; biology; chemistry; metabolism; molecular model; nuclear magnetic resonance spectroscopy; procedures; Amyloid; Binding Sites; Computational Biology; Histidine; Magnetic Resonance Spectroscopy; Metalloproteins; Models, Molecular; Water; Zinc
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160628
作者单位	Lee, M., Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Wang, T., Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Makhlynets, O.V., Department of Chemistry, Syracuse University, yracuse, NY 13244, United States; Wu, Y., Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158, United States; Polizzi, N.F., Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158, United States; Wu, H., Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158, United States; Gosavi, P.M., Department of Chemistry, Syracuse University, yracuse, NY 13244, United States; Stöhr, J., Institute for Neurodegenerative Diseases, University of California, San Francisco, CA 94158, United States, Department of Neurology, University of California, San Francisco, CA 94158, United States; Korendovych, I.V., Department of Chemistr...
推荐引用方式 GB/T 7714	Lee M.,Wang T.,Makhlynets O.V.,et al. Zinc-binding structure of a catalytic amyloid from solid-state NMR[J],2017,114(24).
APA	Lee M..,Wang T..,Makhlynets O.V..,Wu Y..,Polizzi N.F..,...&Hong M..(2017).Zinc-binding structure of a catalytic amyloid from solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America,114(24).
MLA	Lee M.,et al."Zinc-binding structure of a catalytic amyloid from solid-state NMR".Proceedings of the National Academy of Sciences of the United States of America 114.24(2017).