Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp

IF 16.8 1区生物学

Nature Structural &Molecular Biology Pub Date : 2018-01-17 DOI:10.2210/PDB6AXZ/PDB

M. Gallagher-Jones, C. Glynn, D. Boyer, M. Martynowycz, Evelyn Hernandez, Jennifer Miao, Chih-Te Zee, I. Novikova, Lukasz Goldschmidt, Heather T Mcfarlane, G. Helguera, James E. Evans, M. Sawaya, D. Cascio, D. Eisenberg, T. Gonen, José A. Rodríguez

引用次数: 15

Abstract

The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-angstrom-resolution structure of a protofibril formed by a wild-type segment from the β2–α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named ‘polar clasps’.

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朊病毒原纤维的Sub-ångström冷冻电镜结构揭示了极性扣

感染性、蛋白酶抗性、富含β-片和原纤维的哺乳动物朊病毒的原子结构尚不清楚。通过冷冻电镜方法MicroED，我们揭示了由银行田鼠朊病毒蛋白的β2–α2环的野生型片段形成的原纤维的亚埃分辨率结构。这种原纤维的结构揭示了一个稳定的氢键网络，将极性拉链连接在一张纸上，产生我们称之为“极性扣”的图案。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Nature Structural &Molecular Biology 生物-生化与分子生物学

自引率

1.80%

发文量

160

期刊介绍： Nature Structural & Molecular Biology is a monthly journal that focuses on the functional and mechanistic understanding of how molecular components in a biological process work together. It serves as an integrated forum for structural and molecular studies. The journal places a strong emphasis on the functional and mechanistic understanding of how molecular components in a biological process work together. Some specific areas of interest include the structure and function of proteins, nucleic acids, and other macromolecules, DNA replication, repair and recombination, transcription, regulation of transcription and translation, protein folding, processing and degradation, signal transduction, and intracellular signaling.