期刊
PROTEIN SCIENCE
卷 27, 期 9, 页码 1544-1556出版社
WILEY
DOI: 10.1002/pro.3454
关键词
cryo-EM; membrane attack complex (MAC); cholesterol-dependent cytolysin (CDC); anthrax; pore structure; membrane
资金
- NCI NIH HHS [DP2 CA186571] Funding Source: Medline
The beta pore-forming proteins (-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.
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