Advances in structure determination by cryo-EM to unravel membrane-spanning pore formation.
Advances in structure determination by cryo-EM to unravel membrane-spanning pore formation.
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冷冻电镜结构测定的进展揭示了跨膜孔的形成。
DOI：
10.1002/pro.3454
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Taylor,DerekJ
中科院分区：
文献类型：
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作者：
Scott,Harry;Huang,Wei;Bann,JamesG;Taylor,DerekJ
β-孔道形成蛋白(β-PFP)是一大类多肽，由所有生命王国产生，为其物种自身的生存做出贡献。孔组装是一个复杂的多步骤过程，包括受体/膜识别和寡聚事件，随后是大规模的结构重排，促进前孔成熟为跨孔功能膜。传统上，由于缺乏结构数据，对孔的形成、组装和成熟的充分理解一直受到阻碍；特别是对于代表不同构象的功能孔的组装。然而，低温电子显微镜(CRYO-EM)技术的最新进展为描绘这种柔性络合物的结构提供了机会，并且在不同的状态下，达到近原子分辨率。在这篇综述中，我们特别强调使用冷冻-EM来揭示这个家族中一些重要成员的机制细节，包括结构、激活和成熟。
The beta pore‐forming proteins (β‐PFPs) are a large class of polypeptides that are produced by all Kingdoms of life to contribute to their species' own survival. Pore assembly is a sophisticated multi‐step process that includes receptor/membrane recognition and oligomerization events, and is ensued by large‐scale structural rearrangements, which facilitate maturation of a prepore into a functional membrane spanning pore. A full understanding of pore formation, assembly, and maturation has traditionally been hindered by a lack of structural data; particularly for assemblies representing differing conformations of functional pores. However, recent advancements in cryo‐electron microscopy (cryo‐EM) techniques have provided the opportunity to delineate the structures of such flexible complexes, and in different states, to near‐atomic resolution. In this review, we place a particular emphasis on the use of cryo‐EM to uncover the mechanistic details including architecture, activation, and maturation for some of the prominent members of this family.