Advances in structure determination by cryo-EM to unravel membrane-spanning pore formation
Bann, James G.
Taylor, Derek J.
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Scott, H. , Huang, W. , Bann, J. G. and Taylor, D. J. (2018), Advances in structure determination by cryo‐EM to unravel membrane‐spanning pore formation. Protein Science, 27: 1544-1556
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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