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The 3D structure of the fusion primed Sendai F-protein determined by electron cryomicroscopy

By Kai Ludwig, Bolormaa Baljinnyam, Andreas Herrmann and Christoph Böttcher

Abstract

The three dimensional (3D) structure of the ectodomain of the entire fusion mediating F protein from Sendai virus [MW (trimer) ∼177 kDa] has been determined by cryoelectron microscopy of single molecules and subsequent 3D reconstruction at a resolution of ∼16 Å. The reconstruction, which has been obtained from the native, proteolytic processed fusion primed F1+F2 form, shows the protein protruding ∼170 Å out of the membrane in a homotrimeric association. It consists of a defined ∼65 Å wide distal head and an adjacent neck, which is connected to an 70 Å elongated stalk. Although the overall shape appears to be similar to the recently reported X-ray structure of the Newcastle disease virus F protein, a closer comparison reveals structural differences suggesting that the investigated Sendai F structure represents an advanced state towards the fusion active conformation

Topics: Articles
Publisher: Oxford University Press
Year: 2003
DOI identifier: 10.1093/emboj
OAI identifier: oai:pubmedcentral.nih.gov:169058
Provided by: PubMed Central
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